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+24	47	in vitro reconstitution	experimental_method	Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein	TITLE
+88	93	human	species	Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein	TITLE
+94	99	PI4KB	protein	Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein	TITLE
+107	112	ACBD3	protein	Structural insights and in vitro reconstitution of membrane targeting and activation of human PI4KB by the ACBD3 protein	TITLE
+0	34	Phosphatidylinositol 4-kinase beta	protein	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
+36	41	PI4KB	protein	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
+58	63	human	species	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
+64	68	PI4K	protein_type	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
+91	123	phosphatidylinositol 4-phosphate	chemical	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
+125	129	PI4P	chemical	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
+184	194	eukaryotic	taxonomy_domain	Phosphatidylinositol 4-kinase beta (PI4KB) is one of four human PI4K enzymes that generate phosphatidylinositol 4-phosphate (PI4P), a minor but essential regulatory lipid found in all eukaryotic cells.	ABSTRACT
+35	40	PI4Ks	protein_type	To convert their lipid substrates, PI4Ks must be recruited to the correct membrane compartment.	ABSTRACT
+0	5	PI4KB	protein	PI4KB is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools, however, the actual targeting mechanism of PI4KB to the Golgi and TGN membranes is unknown.	ABSTRACT
+81	85	PI4P	chemical	PI4KB is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools, however, the actual targeting mechanism of PI4KB to the Golgi and TGN membranes is unknown.	ABSTRACT
+136	141	PI4KB	protein	PI4KB is critical for the maintenance of the Golgi and trans Golgi network (TGN) PI4P pools, however, the actual targeting mechanism of PI4KB to the Golgi and TGN membranes is unknown.	ABSTRACT
+20	23	NMR	experimental_method	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
+24	33	structure	evidence	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
+52	57	PI4KB	protein	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
+87	108	Golgi adaptor protein	protein_type	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
+109	160	acyl-coenzyme A binding domain containing protein 3	protein	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
+162	167	ACBD3	protein	Here, we present an NMR structure of the complex of PI4KB and its interacting partner, Golgi adaptor protein acyl-coenzyme A binding domain containing protein 3 (ACBD3).	ABSTRACT
+13	18	ACBD3	protein	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
+44	49	PI4KB	protein	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
+123	128	PI4KB	protein	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
+132	137	ACBD3	protein	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
+152	170	enzymatic activity	evidence	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
+184	195	ACBD3:PI4KB	complex_assembly	We show that ACBD3 is capable of recruiting PI4KB to membranes both in vitro and in vivo, and that membrane recruitment of PI4KB by ACBD3 increases its enzymatic activity and that the ACBD3:PI4KB complex formation is essential for proper function of the Golgi.	ABSTRACT
+0	34	Phosphatidylinositol 4-kinase beta	protein	Phosphatidylinositol 4-kinase beta (PI4KB, also known as PI4K IIIβ) is a soluble cytosolic protein yet its function is to phosphorylate membrane lipids.	INTRO
+36	41	PI4KB	protein	Phosphatidylinositol 4-kinase beta (PI4KB, also known as PI4K IIIβ) is a soluble cytosolic protein yet its function is to phosphorylate membrane lipids.	INTRO
+57	66	PI4K IIIβ	protein	Phosphatidylinositol 4-kinase beta (PI4KB, also known as PI4K IIIβ) is a soluble cytosolic protein yet its function is to phosphorylate membrane lipids.	INTRO
+18	23	human	species	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
+24	28	PI4K	protein_type	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
+56	76	phosphatidylinositol	chemical	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
+78	80	PI	chemical	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
+94	126	phosphatidylinositol 4-phosphate	chemical	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
+128	132	PI4P	chemical	It is one of four human PI4K enzymes that phosphorylate phosphatidylinositol (PI) to generate phosphatidylinositol 4-phosphate (PI4P).	INTRO
+0	4	PI4P	chemical	PI4P is an essential lipid found in various membrane compartments including the Golgi and trans-Golgi network (TGN), the plasma membrane and the endocytic compartments.	INTRO
+20	24	PI4P	chemical	In these locations, PI4P plays an important role in cell signaling and lipid transport, and serves as a precursor for higher phosphoinositides or as a docking site for clathrin adaptor or lipid transfer proteins.	INTRO
+125	142	phosphoinositides	chemical	In these locations, PI4P plays an important role in cell signaling and lipid transport, and serves as a precursor for higher phosphoinositides or as a docking site for clathrin adaptor or lipid transfer proteins.	INTRO
+168	176	clathrin	protein_type	In these locations, PI4P plays an important role in cell signaling and lipid transport, and serves as a precursor for higher phosphoinositides or as a docking site for clathrin adaptor or lipid transfer proteins.	INTRO
+16	58	positive-sense single-stranded RNA viruses	taxonomy_domain	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
+60	72	+RNA viruses	taxonomy_domain	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
+109	114	human	species	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
+133	138	human	species	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
+139	144	PI4KA	protein	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
+148	153	PI4KB	protein	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
+183	187	PI4P	chemical	A wide range of positive-sense single-stranded RNA viruses (+RNA viruses), including many that are important human pathogens, hijack human PI4KA or PI4KB enzymes to generate specific PI4P-enriched organelles called membranous webs or replication factories.	INTRO
+6	16	structures	evidence	These structures are essential for effective viral replication.	INTRO
+45	50	viral	taxonomy_domain	These structures are essential for effective viral replication.	INTRO
+26	31	PI4KB	protein	Recently, highly specific PI4KB inhibitors were developed as potential antivirals.	INTRO
+0	4	PI4K	protein_type	PI4K kinases must be recruited to the correct membrane type to fulfill their enzymatic functions.	INTRO
+5	12	kinases	protein_type	PI4K kinases must be recruited to the correct membrane type to fulfill their enzymatic functions.	INTRO
+0	13	Type II PI4Ks	protein_type	Type II PI4Ks (PI4K2A and PI4K2B) are heavily palmitoylated and thus behave as membrane proteins.	INTRO
+15	21	PI4K2A	protein	Type II PI4Ks (PI4K2A and PI4K2B) are heavily palmitoylated and thus behave as membrane proteins.	INTRO
+26	32	PI4K2B	protein	Type II PI4Ks (PI4K2A and PI4K2B) are heavily palmitoylated and thus behave as membrane proteins.	INTRO
+38	59	heavily palmitoylated	protein_state	Type II PI4Ks (PI4K2A and PI4K2B) are heavily palmitoylated and thus behave as membrane proteins.	INTRO
+79	96	membrane proteins	protein	Type II PI4Ks (PI4K2A and PI4K2B) are heavily palmitoylated and thus behave as membrane proteins.	INTRO
+13	27	type III PI4Ks	protein_type	In contrast, type III PI4Ks (PI4KA and PI4KB) are soluble cytosolic proteins that are recruited to appropriate membranes indirectly via protein-protein interactions.	INTRO
+29	34	PI4KA	protein	In contrast, type III PI4Ks (PI4KA and PI4KB) are soluble cytosolic proteins that are recruited to appropriate membranes indirectly via protein-protein interactions.	INTRO
+39	44	PI4KB	protein	In contrast, type III PI4Ks (PI4KA and PI4KB) are soluble cytosolic proteins that are recruited to appropriate membranes indirectly via protein-protein interactions.	INTRO
+19	24	PI4KA	protein	The recruitment of PI4KA to the plasma membrane by EFR3 and TTC7 is relatively well understood even at the structural level, but, the actual molecular mechanism of PI4KB recruitment to the Golgi is still poorly understood.	INTRO
+51	55	EFR3	protein	The recruitment of PI4KA to the plasma membrane by EFR3 and TTC7 is relatively well understood even at the structural level, but, the actual molecular mechanism of PI4KB recruitment to the Golgi is still poorly understood.	INTRO
+60	64	TTC7	protein	The recruitment of PI4KA to the plasma membrane by EFR3 and TTC7 is relatively well understood even at the structural level, but, the actual molecular mechanism of PI4KB recruitment to the Golgi is still poorly understood.	INTRO
+164	169	PI4KB	protein	The recruitment of PI4KA to the plasma membrane by EFR3 and TTC7 is relatively well understood even at the structural level, but, the actual molecular mechanism of PI4KB recruitment to the Golgi is still poorly understood.	INTRO
+0	51	Acyl-coenzyme A binding domain containing protein 3	protein	Acyl-coenzyme A binding domain containing protein 3 (ACBD3, also known as GCP60 and PAP7) is a Golgi resident protein.	INTRO
+53	58	ACBD3	protein	Acyl-coenzyme A binding domain containing protein 3 (ACBD3, also known as GCP60 and PAP7) is a Golgi resident protein.	INTRO
+74	79	GCP60	protein	Acyl-coenzyme A binding domain containing protein 3 (ACBD3, also known as GCP60 and PAP7) is a Golgi resident protein.	INTRO
+84	88	PAP7	protein	Acyl-coenzyme A binding domain containing protein 3 (ACBD3, also known as GCP60 and PAP7) is a Golgi resident protein.	INTRO
+89	98	golgin B1	protein	Its membrane localization is mediated by the interaction with the Golgi integral protein golgin B1/giantin.	INTRO
+99	106	giantin	protein	Its membrane localization is mediated by the interaction with the Golgi integral protein golgin B1/giantin.	INTRO
+0	5	ACBD3	protein	ACBD3 functions as an adaptor protein and signaling hub across cellular signaling pathways.	INTRO
+0	5	ACBD3	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+55	64	golgin A3	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+65	75	golgin-160	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+99	112	Numb proteins	protein_type	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+179	196	metal transporter	protein_type	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+197	201	DMT1	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+206	215	monomeric	oligomeric_state	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+216	225	G protein	protein_type	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+226	233	Dexras1	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+246	250	iron	chemical	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+272	284	lipid kinase	protein_type	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+285	290	PI4KB	protein	ACBD3 can interact with a number of proteins including golgin A3/golgin-160 to regulate apoptosis, Numb proteins to control asymmetric cell division and neuronal differentiation, metal transporter DMT1 and monomeric G protein Dexras1 to maintain iron homeostasis, and the lipid kinase PI4KB to regulate lipid homeostasis.	INTRO
+0	5	ACBD3	protein	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
+138	158	polyglutamine repeat	structure_element	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
+170	176	mutant	protein_state	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
+177	187	huntingtin	protein	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
+215	224	monomeric	oligomeric_state	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
+225	234	G protein	protein_type	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
+235	239	Rhes	protein	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
+240	247	Dexras2	protein	ACBD3 has been also implicated in the pathology of neurodegenerative diseases such as Huntington’s disease due to its interactions with a polyglutamine repeat-containing mutant huntingtin and the striatal-selective monomeric G protein Rhes/Dexras2.	INTRO
+0	5	ACBD3	protein	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
+30	35	viral	taxonomy_domain	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
+36	62	non-structural 3A proteins	protein_type	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
+92	106	picornaviruses	taxonomy_domain	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
+117	127	poliovirus	taxonomy_domain	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
+129	146	coxsackievirus B3	taxonomy_domain	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
+152	163	Aichi virus	taxonomy_domain	ACBD3 is a binding partner of viral non-structural 3A proteins and a host factor of several picornaviruses including poliovirus, coxsackievirus B3, and Aichi virus.	INTRO
+13	56	biochemical and structural characterization	experimental_method	We present a biochemical and structural characterization of the molecular complex composed of the ACBD3 protein and the PI4KB enzyme.	INTRO
+98	103	ACBD3	protein	We present a biochemical and structural characterization of the molecular complex composed of the ACBD3 protein and the PI4KB enzyme.	INTRO
+120	125	PI4KB	protein	We present a biochemical and structural characterization of the molecular complex composed of the ACBD3 protein and the PI4KB enzyme.	INTRO
+13	18	ACBD3	protein	We show that ACBD3 can recruit PI4KB to model membranes as well as redirect PI4KB to cellular membranes where it is not naturally found.	INTRO
+31	36	PI4KB	protein	We show that ACBD3 can recruit PI4KB to model membranes as well as redirect PI4KB to cellular membranes where it is not naturally found.	INTRO
+76	81	PI4KB	protein	We show that ACBD3 can recruit PI4KB to model membranes as well as redirect PI4KB to cellular membranes where it is not naturally found.	INTRO
+24	29	ACBD3	protein	Our data also show that ACBD3 regulates the enzymatic activity of PI4KB kinase through membrane recruitment rather than allostery.	INTRO
+44	62	enzymatic activity	evidence	Our data also show that ACBD3 regulates the enzymatic activity of PI4KB kinase through membrane recruitment rather than allostery.	INTRO
+66	71	PI4KB	protein	Our data also show that ACBD3 regulates the enzymatic activity of PI4KB kinase through membrane recruitment rather than allostery.	INTRO
+72	78	kinase	protein_type	Our data also show that ACBD3 regulates the enzymatic activity of PI4KB kinase through membrane recruitment rather than allostery.	INTRO
+0	5	ACBD3	protein	ACBD3 and PI4KB interact with 1:1 stoichiometry with submicromolar affinity	RESULTS
+10	15	PI4KB	protein	ACBD3 and PI4KB interact with 1:1 stoichiometry with submicromolar affinity	RESULTS
+44	49	ACBD3	protein	In order to verify the interactions between ACBD3 and PI4KB we expressed and purified both proteins.	RESULTS
+54	59	PI4KB	protein	In order to verify the interactions between ACBD3 and PI4KB we expressed and purified both proteins.	RESULTS
+63	85	expressed and purified	experimental_method	In order to verify the interactions between ACBD3 and PI4KB we expressed and purified both proteins.	RESULTS
+22	42	bacterial expression	experimental_method	To increase yields of bacterial expression the intrinsically disordered region of PI4KB (residues 423–522) was removed (Fig. 1A).	RESULTS
+47	78	intrinsically disordered region	structure_element	To increase yields of bacterial expression the intrinsically disordered region of PI4KB (residues 423–522) was removed (Fig. 1A).	RESULTS
+82	87	PI4KB	protein	To increase yields of bacterial expression the intrinsically disordered region of PI4KB (residues 423–522) was removed (Fig. 1A).	RESULTS
+98	105	423–522	residue_range	To increase yields of bacterial expression the intrinsically disordered region of PI4KB (residues 423–522) was removed (Fig. 1A).	RESULTS
+111	118	removed	experimental_method	To increase yields of bacterial expression the intrinsically disordered region of PI4KB (residues 423–522) was removed (Fig. 1A).	RESULTS
+14	22	deletion	experimental_method	This internal deletion does not significantly affect the kinase activity(SI Fig. 1A) or interaction with ACBD3 (SI Fig. 1B,C).	RESULTS
+57	63	kinase	protein_type	This internal deletion does not significantly affect the kinase activity(SI Fig. 1A) or interaction with ACBD3 (SI Fig. 1B,C).	RESULTS
+105	110	ACBD3	protein	This internal deletion does not significantly affect the kinase activity(SI Fig. 1A) or interaction with ACBD3 (SI Fig. 1B,C).	RESULTS
+6	28	in vitro binding assay	experimental_method	In an in vitro binding assay, ACBD3 co-purified with the NiNTA-immobilized N-terminal His6GB1-tagged PI4KB (Fig. 1B, left panel), suggesting a direct interaction.	RESULTS
+30	35	ACBD3	protein	In an in vitro binding assay, ACBD3 co-purified with the NiNTA-immobilized N-terminal His6GB1-tagged PI4KB (Fig. 1B, left panel), suggesting a direct interaction.	RESULTS
+36	74	co-purified with the NiNTA-immobilized	experimental_method	In an in vitro binding assay, ACBD3 co-purified with the NiNTA-immobilized N-terminal His6GB1-tagged PI4KB (Fig. 1B, left panel), suggesting a direct interaction.	RESULTS
+86	100	His6GB1-tagged	protein_state	In an in vitro binding assay, ACBD3 co-purified with the NiNTA-immobilized N-terminal His6GB1-tagged PI4KB (Fig. 1B, left panel), suggesting a direct interaction.	RESULTS
+101	106	PI4KB	protein	In an in vitro binding assay, ACBD3 co-purified with the NiNTA-immobilized N-terminal His6GB1-tagged PI4KB (Fig. 1B, left panel), suggesting a direct interaction.	RESULTS
+8	34	mammalian two-hybrid assay	experimental_method	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
+60	69	localized	evidence	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
+94	102	Q domain	structure_element	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
+106	111	ACBD3	protein	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
+152	161	glutamine	residue_name	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
+180	197	N-terminal region	structure_element	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
+201	206	PI4KB	protein	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
+221	235	helical domain	structure_element	Using a mammalian two-hybrid assay Greninger and colleagues localized this interaction to the Q domain of ACBD3 (named according to its high content of glutamine residues) and the N-terminal region of PI4KB preceding its helical domain.	RESULTS
+3	12	expressed	experimental_method	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
+17	25	Q domain	structure_element	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
+29	34	ACBD3	protein	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
+45	52	241–308	residue_range	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
+62	79	N-terminal region	structure_element	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
+83	88	PI4KB	protein	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
+99	103	1–68	residue_range	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
+108	115	E. coli	species	We expressed the Q domain of ACBD3 (residues 241–308) and the N-terminal region of PI4KB (residues 1–68) in E. coli and using purified recombinant proteins, we confirmed that these two domains are sufficient to maintain the interaction (Fig. 1B, middle and right panel).	RESULTS
+34	39	ACBD3	protein	Because it has been reported that ACBD3 can dimerize in a mammalian two-hybrid assay, we were interested in determining the stoichiometry of the ACBD3:PI4KB protein complex.	RESULTS
+44	52	dimerize	oligomeric_state	Because it has been reported that ACBD3 can dimerize in a mammalian two-hybrid assay, we were interested in determining the stoichiometry of the ACBD3:PI4KB protein complex.	RESULTS
+58	84	mammalian two-hybrid assay	experimental_method	Because it has been reported that ACBD3 can dimerize in a mammalian two-hybrid assay, we were interested in determining the stoichiometry of the ACBD3:PI4KB protein complex.	RESULTS
+145	156	ACBD3:PI4KB	complex_assembly	Because it has been reported that ACBD3 can dimerize in a mammalian two-hybrid assay, we were interested in determining the stoichiometry of the ACBD3:PI4KB protein complex.	RESULTS
+4	30	sedimentation coefficients	evidence	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
+34	39	ACBD3	protein	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
+44	49	PI4KB	protein	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
+50	55	alone	protein_state	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
+60	71	ACBD3:PI4KB	complex_assembly	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
+99	129	analytical ultracentrifugation	experimental_method	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
+198	215	molecular weights	evidence	The sedimentation coefficients of ACBD3 and PI4KB alone, or ACBD3:PI4KB complex were determined by analytical ultracentrifugation and found to be 3.1 S, 4.1 S, and 5.1 S. These values correspond to molecular weights of approximately 55 kDa, 80 kDa, and 130 kDa, respectively.	RESULTS
+44	53	monomeric	oligomeric_state	This result suggests that both proteins are monomeric and the stoichiometry of the ACBD3: PI4KB protein complex is 1:1 (Fig. 1C, left panel).	RESULTS
+83	95	ACBD3: PI4KB	complex_assembly	This result suggests that both proteins are monomeric and the stoichiometry of the ACBD3: PI4KB protein complex is 1:1 (Fig. 1C, left panel).	RESULTS
+53	61	Q domain	structure_element	Similar results were obtained for the complex of the Q domain of ACBD3 and the N-terminal region of PI4KB (Fig. 1C, right panel).	RESULTS
+65	70	ACBD3	protein	Similar results were obtained for the complex of the Q domain of ACBD3 and the N-terminal region of PI4KB (Fig. 1C, right panel).	RESULTS
+79	96	N-terminal region	structure_element	Similar results were obtained for the complex of the Q domain of ACBD3 and the N-terminal region of PI4KB (Fig. 1C, right panel).	RESULTS
+100	105	PI4KB	protein	Similar results were obtained for the complex of the Q domain of ACBD3 and the N-terminal region of PI4KB (Fig. 1C, right panel).	RESULTS
+71	82	full length	protein_state	We also determined the strength of the interaction between recombinant full length ACBD3 and PI4KB using surface plasmon resonance (SPR).	RESULTS
+83	88	ACBD3	protein	We also determined the strength of the interaction between recombinant full length ACBD3 and PI4KB using surface plasmon resonance (SPR).	RESULTS
+93	98	PI4KB	protein	We also determined the strength of the interaction between recombinant full length ACBD3 and PI4KB using surface plasmon resonance (SPR).	RESULTS
+105	130	surface plasmon resonance	experimental_method	We also determined the strength of the interaction between recombinant full length ACBD3 and PI4KB using surface plasmon resonance (SPR).	RESULTS
+132	135	SPR	experimental_method	We also determined the strength of the interaction between recombinant full length ACBD3 and PI4KB using surface plasmon resonance (SPR).	RESULTS
+0	3	SPR	experimental_method	SPR measurements revealed a strong interaction with a Kd value of 320 +/−130 nM (Fig. 1D, SI Fig. 1D).	RESULTS
+54	56	Kd	evidence	SPR measurements revealed a strong interaction with a Kd value of 320 +/−130 nM (Fig. 1D, SI Fig. 1D).	RESULTS
+18	23	ACBD3	protein	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
+28	33	PI4KB	protein	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
+64	72	Q domain	structure_element	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
+76	81	ACBD3	protein	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
+90	107	N-terminal region	structure_element	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
+111	116	PI4KB	protein	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
+146	167	dissociation constant	evidence	We concluded that ACBD3 and PI4KB interact directly through the Q domain of ACBD3 and the N-terminal region of PI4KB forming a 1:1 complex with a dissociation constant in the submicromolar range.	RESULTS
+0	19	Structural analysis	experimental_method	Structural analysis of the ACBD3:PI4KB complex	RESULTS
+27	38	ACBD3:PI4KB	complex_assembly	Structural analysis of the ACBD3:PI4KB complex	RESULTS
+0	11	Full length	protein_state	Full length ACBD3 and PI4KB both contain large intrinsically disordered regions that impede crystallization.	RESULTS
+12	17	ACBD3	protein	Full length ACBD3 and PI4KB both contain large intrinsically disordered regions that impede crystallization.	RESULTS
+22	27	PI4KB	protein	Full length ACBD3 and PI4KB both contain large intrinsically disordered regions that impede crystallization.	RESULTS
+47	79	intrinsically disordered regions	structure_element	Full length ACBD3 and PI4KB both contain large intrinsically disordered regions that impede crystallization.	RESULTS
+8	53	hydrogen-deuterium exchange mass spectrometry	experimental_method	We used hydrogen-deuterium exchange mass spectrometry (HDX-MS) analysis of the complex to determine which parts of the complex are well folded (SI Fig. 2).	RESULTS
+55	61	HDX-MS	experimental_method	We used hydrogen-deuterium exchange mass spectrometry (HDX-MS) analysis of the complex to determine which parts of the complex are well folded (SI Fig. 2).	RESULTS
+131	142	well folded	protein_state	We used hydrogen-deuterium exchange mass spectrometry (HDX-MS) analysis of the complex to determine which parts of the complex are well folded (SI Fig. 2).	RESULTS
+34	42	crystals	evidence	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
+73	82	truncated	protein_state	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
+117	122	ACBD3	protein	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
+123	131	Q domain	structure_element	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
+140	157	N-terminal region	structure_element	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
+161	166	PI4KB	protein	However, we were unable to obtain crystals even when using significantly truncated constructs that included only the ACBD3 Q domain and the N-terminal region of PI4KB.	RESULTS
+32	52	isotopically labeled	protein_state	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
+53	58	ACBD3	protein	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
+59	67	Q domain	structure_element	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
+72	92	isotopically labeled	protein_state	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
+93	98	ACBD3	protein	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
+99	107	Q domain	structure_element	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
+108	113	PI4KB	protein	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
+114	131	N-terminal region	structure_element	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
+157	173	NMR spectroscopy	experimental_method	For this reason, we produced an isotopically labeled ACBD3 Q domain and isotopically labeled ACBD3 Q domain:PI4KB N-terminal region protein complex and used NMR spectroscopy for structural characterization.	RESULTS
+7	24	N-terminal region	structure_element	As the N-terminal region protein complex was prepared by co-expression of both proteins, the samples consisted of an equimolar mixture of two uniformly 15N/13C labelled molecules.	RESULTS
+57	70	co-expression	experimental_method	As the N-terminal region protein complex was prepared by co-expression of both proteins, the samples consisted of an equimolar mixture of two uniformly 15N/13C labelled molecules.	RESULTS
+152	155	15N	chemical	As the N-terminal region protein complex was prepared by co-expression of both proteins, the samples consisted of an equimolar mixture of two uniformly 15N/13C labelled molecules.	RESULTS
+156	159	13C	chemical	As the N-terminal region protein complex was prepared by co-expression of both proteins, the samples consisted of an equimolar mixture of two uniformly 15N/13C labelled molecules.	RESULTS
+160	168	labelled	protein_state	As the N-terminal region protein complex was prepared by co-expression of both proteins, the samples consisted of an equimolar mixture of two uniformly 15N/13C labelled molecules.	RESULTS
+68	72	free	protein_state	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
+73	78	ACBD3	protein	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
+79	87	Q domain	structure_element	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
+127	141	2D 15N/1H HSQC	experimental_method	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
+142	149	spectra	evidence	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
+215	243	triple-resonance experiments	experimental_method	Comprehensive backbone and side-chain resonance assignments for the free ACBD3 Q domain and the complex, as illustrated by the 2D 15N/1H HSQC spectra (SI Figs 3 and 4), were obtained using a standard combination of triple-resonance experiments, as described previously.	RESULTS
+24	27	15N	chemical	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
+32	34	1H	chemical	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
+44	48	free	protein_state	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
+49	54	ACBD3	protein	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
+55	63	Q domain	structure_element	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
+143	152	Met1-Lys4	residue_range	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
+158	163	Gln44	residue_name_number	Backbone amide signals (15N and 1H) for the free ACBD3 Q domain were nearly completely assigned apart from the first four N-terminal residues (Met1-Lys4) and Gln44.	RESULTS
+70	74	free	protein_state	Over 93% of non-exchangeable side-chain signals were assigned for the free ACBD3 Q domain.	RESULTS
+75	80	ACBD3	protein	Over 93% of non-exchangeable side-chain signals were assigned for the free ACBD3 Q domain.	RESULTS
+81	89	Q domain	structure_element	Over 93% of non-exchangeable side-chain signals were assigned for the free ACBD3 Q domain.	RESULTS
+85	88	Gln	residue_name	Apart from the four N-terminal residues, the side-chain assignments were missing for Gln (Hg3), Gln (Ha/Hb/Hg), Gln44 (Ha/Hb/Hg) and Gln48 (Hg) mainly due to extensive overlaps within the spectral regions populated by highly abundant glutamine side-chain resonances.	RESULTS
+96	99	Gln	residue_name	Apart from the four N-terminal residues, the side-chain assignments were missing for Gln (Hg3), Gln (Ha/Hb/Hg), Gln44 (Ha/Hb/Hg) and Gln48 (Hg) mainly due to extensive overlaps within the spectral regions populated by highly abundant glutamine side-chain resonances.	RESULTS
+112	117	Gln44	residue_name_number	Apart from the four N-terminal residues, the side-chain assignments were missing for Gln (Hg3), Gln (Ha/Hb/Hg), Gln44 (Ha/Hb/Hg) and Gln48 (Hg) mainly due to extensive overlaps within the spectral regions populated by highly abundant glutamine side-chain resonances.	RESULTS
+133	138	Gln48	residue_name_number	Apart from the four N-terminal residues, the side-chain assignments were missing for Gln (Hg3), Gln (Ha/Hb/Hg), Gln44 (Ha/Hb/Hg) and Gln48 (Hg) mainly due to extensive overlaps within the spectral regions populated by highly abundant glutamine side-chain resonances.	RESULTS
+234	243	glutamine	residue_name	Apart from the four N-terminal residues, the side-chain assignments were missing for Gln (Hg3), Gln (Ha/Hb/Hg), Gln44 (Ha/Hb/Hg) and Gln48 (Hg) mainly due to extensive overlaps within the spectral regions populated by highly abundant glutamine side-chain resonances.	RESULTS
+53	60	spectra	evidence	The protein complex yielded relatively well resolved spectra (SI Fig. 4) that resulted in assignment of backbone amide signals for all residues apart from Gln (ACBD3) and Ala2 (PI4KB).	RESULTS
+155	158	Gln	residue_name	The protein complex yielded relatively well resolved spectra (SI Fig. 4) that resulted in assignment of backbone amide signals for all residues apart from Gln (ACBD3) and Ala2 (PI4KB).	RESULTS
+160	165	ACBD3	protein	The protein complex yielded relatively well resolved spectra (SI Fig. 4) that resulted in assignment of backbone amide signals for all residues apart from Gln (ACBD3) and Ala2 (PI4KB).	RESULTS
+171	175	Ala2	residue_name_number	The protein complex yielded relatively well resolved spectra (SI Fig. 4) that resulted in assignment of backbone amide signals for all residues apart from Gln (ACBD3) and Ala2 (PI4KB).	RESULTS
+177	182	PI4KB	protein	The protein complex yielded relatively well resolved spectra (SI Fig. 4) that resulted in assignment of backbone amide signals for all residues apart from Gln (ACBD3) and Ala2 (PI4KB).	RESULTS
+25	28	15N	chemical	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
+30	33	13C	chemical	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
+38	40	1H	chemical	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
+99	103	NOEs	evidence	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
+122	142	3D 15N/1H NOESY-HSQC	experimental_method	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
+147	164	13C/1H HMQC-NOESY	experimental_method	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
+165	172	spectra	evidence	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
+204	226	structural calculation	experimental_method	The essentially complete 15N, 13C and 1H resonance assignments allowed automated assignment of the NOEs identified in the 3D 15N/1H NOESY-HSQC and 13C/1H HMQC-NOESY spectra that were subsequently used in structural calculation.	RESULTS
+0	21	Structural statistics	evidence	Structural statistics for the final water-refined sets of structures are shown in SI Table 1.	RESULTS
+58	68	structures	evidence	Structural statistics for the final water-refined sets of structures are shown in SI Table 1.	RESULTS
+5	14	structure	evidence	This structure revealed that the Q domain forms a two helix hairpin.	RESULTS
+33	41	Q domain	structure_element	This structure revealed that the Q domain forms a two helix hairpin.	RESULTS
+50	67	two helix hairpin	structure_element	This structure revealed that the Q domain forms a two helix hairpin.	RESULTS
+10	15	helix	structure_element	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
+46	51	helix	structure_element	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
+84	102	three helix bundle	structure_element	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
+133	138	helix	structure_element	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
+146	151	PI4KB	protein	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
+173	178	44–64	residue_range	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
+218	230	kinase helix	structure_element	The first helix bends sharply over the second helix and creates a fold resembling a three helix bundle that serves as a nest for one helix of the PI4KB N-terminus (residues 44–64, from this point on referred to as the kinase helix) (Fig. 2A).	RESULTS
+14	26	kinase helix	structure_element	Preceding the kinase helix are three ordered residues (Val42, Ile43, and Asp44) that also contribute to the interaction (Fig. 2B).	RESULTS
+55	60	Val42	residue_name_number	Preceding the kinase helix are three ordered residues (Val42, Ile43, and Asp44) that also contribute to the interaction (Fig. 2B).	RESULTS
+62	67	Ile43	residue_name_number	Preceding the kinase helix are three ordered residues (Val42, Ile43, and Asp44) that also contribute to the interaction (Fig. 2B).	RESULTS
+73	78	Asp44	residue_name_number	Preceding the kinase helix are three ordered residues (Val42, Ile43, and Asp44) that also contribute to the interaction (Fig. 2B).	RESULTS
+26	31	PI4KB	protein	The remaining part of the PI4KB N-termini, however, is disordered (SI Fig. 5).	RESULTS
+18	29	PI4KB:ACBD3	complex_assembly	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
+30	58	interactions are hydrophobic	bond_interaction	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
+81	95	hydrogen bonds	bond_interaction	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
+123	128	ACBD3	protein	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
+129	135	Tyr261	residue_name_number	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
+140	145	PI4KB	protein	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
+146	151	His63	residue_name_number	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
+182	187	ACBD3	protein	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
+188	194	Tyr288	residue_name_number	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
+203	208	PI4KB	protein	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
+219	224	Asp44	residue_name_number	Almost all of the PI4KB:ACBD3 interactions are hydrophobic with the exception of hydrogen bonds between the side chains of ACBD3 Tyr261 and PI4KB His63, and between the sidechain of ACBD3 Tyr288 and the PI4KB backbone (Asp44) (Fig. 2B).	RESULTS
+33	38	PI4KB	protein	Interestingly, we noted that the PI4KB helix is amphipathic and its hydrophobic surface leans on the Q domain (Fig. 2C).	RESULTS
+39	44	helix	structure_element	Interestingly, we noted that the PI4KB helix is amphipathic and its hydrophobic surface leans on the Q domain (Fig. 2C).	RESULTS
+48	59	amphipathic	protein_state	Interestingly, we noted that the PI4KB helix is amphipathic and its hydrophobic surface leans on the Q domain (Fig. 2C).	RESULTS
+68	87	hydrophobic surface	site	Interestingly, we noted that the PI4KB helix is amphipathic and its hydrophobic surface leans on the Q domain (Fig. 2C).	RESULTS
+101	109	Q domain	structure_element	Interestingly, we noted that the PI4KB helix is amphipathic and its hydrophobic surface leans on the Q domain (Fig. 2C).	RESULTS
+19	34	structural data	evidence	To corroborate the structural data, we introduced a number of point mutations and validated their effect on complex formation using an in vitro pull-down assay (Fig. 2D).	RESULTS
+39	49	introduced	experimental_method	To corroborate the structural data, we introduced a number of point mutations and validated their effect on complex formation using an in vitro pull-down assay (Fig. 2D).	RESULTS
+62	77	point mutations	experimental_method	To corroborate the structural data, we introduced a number of point mutations and validated their effect on complex formation using an in vitro pull-down assay (Fig. 2D).	RESULTS
+135	159	in vitro pull-down assay	experimental_method	To corroborate the structural data, we introduced a number of point mutations and validated their effect on complex formation using an in vitro pull-down assay (Fig. 2D).	RESULTS
+0	9	Wild type	protein_state	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+10	15	ACBD3	protein	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+24	35	co-purified	experimental_method	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+72	83	His6-tagged	protein_state	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+84	93	wild type	protein_state	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+94	99	PI4KB	protein	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+120	125	PI4KB	protein	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+126	130	V42A	mutant	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+135	139	V47A	mutant	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+140	147	mutants	protein_state	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+162	169	mutants	protein_state	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+190	207	binding interface	site	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+209	213	I43A	mutant	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+215	219	V55A	mutant	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+221	225	L56A	mutant	Wild type ACBD3 protein co-purified together with the NiNTA-immobilized His6-tagged wild type PI4KB as well as with the PI4KB V42A and V47A mutants, but not with mutants within the imminent binding interface (I43A, V55A, L56A).	RESULTS
+14	23	wild type	protein_state	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
+24	29	PI4KB	protein	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
+50	55	ACBD3	protein	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
+56	61	Y266A	mutant	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
+62	68	mutant	protein_state	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
+91	96	Y285A	mutant	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
+97	103	mutant	protein_state	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
+122	127	F258A	mutant	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
+129	134	H284A	mutant	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
+140	145	Y288A	mutant	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
+146	153	mutants	protein_state	As predicted, wild type PI4KB interacted with the ACBD3 Y266A mutant and slightly with the Y285A mutant, but not with the F258A, H284A, and Y288A mutants (Fig. 2D).	RESULTS
+0	5	ACBD3	protein	ACBD3 efficiently recruits the PI4KB enzyme to membranes	RESULTS
+31	36	PI4KB	protein	ACBD3 efficiently recruits the PI4KB enzyme to membranes	RESULTS
+35	46	ACBD3:PI4KB	complex_assembly	We next sought to determine if the ACBD3:PI4KB interaction drives membrane localization of the PI4KB enzyme.	RESULTS
+95	100	PI4KB	protein	We next sought to determine if the ACBD3:PI4KB interaction drives membrane localization of the PI4KB enzyme.	RESULTS
+36	72	in vitro membrane recruitment system	experimental_method	To do this, we first established an in vitro membrane recruitment system using Giant Unilamellar Vesicles (GUVs) containing the PI4KB substrate – the PI lipid.	RESULTS
+79	105	Giant Unilamellar Vesicles	experimental_method	To do this, we first established an in vitro membrane recruitment system using Giant Unilamellar Vesicles (GUVs) containing the PI4KB substrate – the PI lipid.	RESULTS
+107	111	GUVs	experimental_method	To do this, we first established an in vitro membrane recruitment system using Giant Unilamellar Vesicles (GUVs) containing the PI4KB substrate – the PI lipid.	RESULTS
+128	133	PI4KB	protein	To do this, we first established an in vitro membrane recruitment system using Giant Unilamellar Vesicles (GUVs) containing the PI4KB substrate – the PI lipid.	RESULTS
+150	152	PI	chemical	To do this, we first established an in vitro membrane recruitment system using Giant Unilamellar Vesicles (GUVs) containing the PI4KB substrate – the PI lipid.	RESULTS
+17	22	PI4KB	protein	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
+23	29	kinase	protein_type	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
+47	56	localized	evidence	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
+75	79	GUVs	experimental_method	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
+139	144	ACBD3	protein	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
+167	171	GUVs	experimental_method	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
+195	200	ACBD3	protein	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
+209	227	DGS-NTA (Ni) lipid	chemical	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
+246	251	PI4KB	protein	We observed that PI4KB kinase was not membrane localized when added to the GUVs at 600 nM concentration, whereas non-covalent tethering of ACBD3 to the surface of the GUVs, using the His6 tag on ACBD3 and the DGS-NTA (Ni) lipid, led to efficient PI4KB membrane localization (Fig. 3A).	RESULTS
+24	29	ACBD3	protein	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
+55	75	localization signals	evidence	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
+80	85	PI4KB	protein	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
+87	101	overexpression	experimental_method	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
+109	117	Q domain	structure_element	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
+163	169	kinase	protein_type	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
+224	229	PI4KB	protein	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
+259	273	overexpressing	experimental_method	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
+278	281	GFP	experimental_method	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
+284	292	Q domain	structure_element	We hypothesized that if ACBD3 is one of the main Golgi localization signals for PI4KB, overexpression of the Q domain should decrease the amount of the endogenous kinase on the Golgi. Indeed, we observed loss for endogenous PI4KB signal on the Golgi in cells overexpressing the GFP – Q domain construct (Fig. 3B upper panel).	RESULTS
+25	31	signal	evidence	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
+67	73	kinase	protein_type	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
+179	185	signal	evidence	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
+194	208	overexpression	experimental_method	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
+212	215	GFP	experimental_method	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
+227	238	non-binding	protein_state	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
+239	247	Q domain	structure_element	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
+248	254	mutant	protein_state	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
+276	288	localization	evidence	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
+307	312	PI4KB	protein	We attribute the loss of signal to the immunostaining protocol-the kinase that is not bound to Golgi is lost during the permeabilization step and hence the “disappearance” of the signal because overexpression of GFP alone or a non-binding Q domain mutant has no effect on the localization of the endogenous PI4KB (Fig. 3B).	RESULTS
+19	33	overexpression	experimental_method	Given this result, overexpression of the Q domain should also interfere with the PI4KB dependent Golgi functions.	RESULTS
+41	49	Q domain	structure_element	Given this result, overexpression of the Q domain should also interfere with the PI4KB dependent Golgi functions.	RESULTS
+81	86	PI4KB	protein	Given this result, overexpression of the Q domain should also interfere with the PI4KB dependent Golgi functions.	RESULTS
+0	8	Ceramide	chemical	Ceramide transport and accumulation in Golgi is a well-known PI4KB dependent process.	RESULTS
+61	66	PI4KB	protein	Ceramide transport and accumulation in Golgi is a well-known PI4KB dependent process.	RESULTS
+13	34	fluorescently labeled	protein_state	We have used fluorescently labeled ceramide and analyzed its trafficking in non-transfected cells and cell overexpressing the Q domain.	RESULTS
+35	43	ceramide	chemical	We have used fluorescently labeled ceramide and analyzed its trafficking in non-transfected cells and cell overexpressing the Q domain.	RESULTS
+107	121	overexpressing	experimental_method	We have used fluorescently labeled ceramide and analyzed its trafficking in non-transfected cells and cell overexpressing the Q domain.	RESULTS
+126	134	Q domain	structure_element	We have used fluorescently labeled ceramide and analyzed its trafficking in non-transfected cells and cell overexpressing the Q domain.	RESULTS
+39	47	ceramide	chemical	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
+74	84	expressing	experimental_method	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
+89	91	wt	protein_state	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
+92	100	Q domain	structure_element	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
+124	127	RFP	experimental_method	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
+135	141	mutant	protein_state	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
+142	150	Q domain	structure_element	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
+163	171	ceramide	chemical	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
+207	218	ACBD3:PI4KB	complex_assembly	As expected, the Golgi accumulation of ceramide was not observed in cells expressing the wt Q domain while cells expressing RFP or the mutant Q domain accumulated ceramide normally (Fig. 3C) suggesting that ACBD3:PI4KB complex formation is crucial for the normal function of Golgi.	RESULTS
+36	47	ACBD3:PI4KB	complex_assembly	We further analyzed the function of ACBD3:PI4KB interaction in membrane recruitment of PI4KB in living cells using fluorescently tagged proteins.	RESULTS
+87	92	PI4KB	protein	We further analyzed the function of ACBD3:PI4KB interaction in membrane recruitment of PI4KB in living cells using fluorescently tagged proteins.	RESULTS
+115	135	fluorescently tagged	protein_state	We further analyzed the function of ACBD3:PI4KB interaction in membrane recruitment of PI4KB in living cells using fluorescently tagged proteins.	RESULTS
+12	21	rapamycin	chemical	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
+52	58	FKBP12	protein	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
+60	84	FK506 binding protein 12	protein	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
+90	93	FRB	structure_element	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
+95	103	fragment	structure_element	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
+107	111	mTOR	protein	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
+123	132	rapamycin	chemical	We used the rapamycin-inducible heteromerization of FKBP12 (FK506 binding protein 12) and FRB (fragment of mTOR that binds rapamycin) system.	RESULTS
+3	8	fused	experimental_method	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
+13	16	FRB	structure_element	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
+29	34	34–63	residue_range	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
+42	75	mitochondrial localization signal	structure_element	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
+81	120	mitochondrial A-kinase anchor protein 1	protein	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
+122	127	AKAP1	protein	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
+133	136	CFP	experimental_method	We fused the FRB to residues 34–63 of the mitochondrial localization signal from mitochondrial A-kinase anchor protein 1 (AKAP1) and CFP.	RESULTS
+4	9	ACBD3	protein	The ACBD3 Q domain was then fused to FKBP12 and mRFP (Fig. 3D).	RESULTS
+10	18	Q domain	structure_element	The ACBD3 Q domain was then fused to FKBP12 and mRFP (Fig. 3D).	RESULTS
+28	36	fused to	experimental_method	The ACBD3 Q domain was then fused to FKBP12 and mRFP (Fig. 3D).	RESULTS
+37	43	FKBP12	protein	The ACBD3 Q domain was then fused to FKBP12 and mRFP (Fig. 3D).	RESULTS
+48	52	mRFP	experimental_method	The ACBD3 Q domain was then fused to FKBP12 and mRFP (Fig. 3D).	RESULTS
+12	24	localization	evidence	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
+32	37	ACBD3	protein	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
+38	46	Q domain	structure_element	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
+51	54	GFP	experimental_method	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
+57	62	PI4KB	protein	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
+96	105	rapamycin	chemical	We analyzed localization of the ACBD3 Q domain and GFP – PI4KB before and after the addition of rapamycin.	RESULTS
+21	26	H284A	mutant	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
+27	33	mutant	protein_state	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
+41	46	ACBD3	protein	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
+47	55	Q domain	structure_element	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
+89	94	PI4KB	protein	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
+95	101	kinase	protein_type	As a control we used H284A mutant of the ACBD3 Q domain that does not significantly bind PI4KB kinase.	RESULTS
+18	23	ACDB3	protein	In every case the ACDB3 Q domain was rapidly (within 5 minutes) recruited to the mitochondrial membrane upon addition of rapamycin, but only the wild-type protein effectively directed the kinase to the mitochondria (Fig. 3E, Movie 1 and 2).	RESULTS
+24	32	Q domain	structure_element	In every case the ACDB3 Q domain was rapidly (within 5 minutes) recruited to the mitochondrial membrane upon addition of rapamycin, but only the wild-type protein effectively directed the kinase to the mitochondria (Fig. 3E, Movie 1 and 2).	RESULTS
+121	130	rapamycin	chemical	In every case the ACDB3 Q domain was rapidly (within 5 minutes) recruited to the mitochondrial membrane upon addition of rapamycin, but only the wild-type protein effectively directed the kinase to the mitochondria (Fig. 3E, Movie 1 and 2).	RESULTS
+145	154	wild-type	protein_state	In every case the ACDB3 Q domain was rapidly (within 5 minutes) recruited to the mitochondrial membrane upon addition of rapamycin, but only the wild-type protein effectively directed the kinase to the mitochondria (Fig. 3E, Movie 1 and 2).	RESULTS
+188	194	kinase	protein_type	In every case the ACDB3 Q domain was rapidly (within 5 minutes) recruited to the mitochondrial membrane upon addition of rapamycin, but only the wild-type protein effectively directed the kinase to the mitochondria (Fig. 3E, Movie 1 and 2).	RESULTS
+35	38	GFP	experimental_method	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
+39	44	PI4KB	protein	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
+45	51	kinase	protein_type	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
+55	67	co-expressed	experimental_method	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
+77	86	wild-type	protein_state	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
+87	92	ACDB3	protein	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
+93	101	Q domain	structure_element	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
+129	141	localization	evidence	Notably, we observed that when the GFP-PI4KB kinase is co-expressed with the wild-type ACDB3 Q domain it loses its typical Golgi localization (Fig. 3E upper panel).	RESULTS
+9	14	PI4KB	protein	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
+32	44	localization	evidence	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
+50	62	co-expressed	experimental_method	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
+72	87	non-interacting	protein_state	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
+88	96	Q domain	structure_element	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
+97	103	mutant	protein_state	However, PI4KB retains it Golgi localization when co-expressed with the non-interacting Q domain mutant (Fig. 3E lower panel).	RESULTS
+0	5	ACBD3	protein	ACBD3 increases PI4KB enzymatic activity by recruiting PI4KB to close vicinity of its substrate	RESULTS
+16	21	PI4KB	protein	ACBD3 increases PI4KB enzymatic activity by recruiting PI4KB to close vicinity of its substrate	RESULTS
+22	40	enzymatic activity	evidence	ACBD3 increases PI4KB enzymatic activity by recruiting PI4KB to close vicinity of its substrate	RESULTS
+55	60	PI4KB	protein	ACBD3 increases PI4KB enzymatic activity by recruiting PI4KB to close vicinity of its substrate	RESULTS
+16	21	ACBD3	protein	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
+36	41	PI4KB	protein	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
+42	48	kinase	protein_type	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
+49	67	enzymatic activity	evidence	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
+92	116	luminescent kinase assay	experimental_method	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
+123	125	PI	chemical	To test whether ACBD3 can stimulate PI4KB kinase enzymatic activity we performed a standard luminescent kinase assay using PI-containing micelles as the substrate.	RESULTS
+29	35	kinase	protein_type	We observed no effect on the kinase activity of PI4KB (Fig. 4A) suggesting that ACBD3 does not directly affect the enzyme (e.g. induction of a conformation change).	RESULTS
+48	53	PI4KB	protein	We observed no effect on the kinase activity of PI4KB (Fig. 4A) suggesting that ACBD3 does not directly affect the enzyme (e.g. induction of a conformation change).	RESULTS
+80	85	ACBD3	protein	We observed no effect on the kinase activity of PI4KB (Fig. 4A) suggesting that ACBD3 does not directly affect the enzyme (e.g. induction of a conformation change).	RESULTS
+17	22	ACBD3	protein	However, in vivo ACBD3 is located at the Golgi membranes, whereas in this experiment, ACBD3 was located in the solution and PI is provided as micelles.	RESULTS
+86	91	ACBD3	protein	However, in vivo ACBD3 is located at the Golgi membranes, whereas in this experiment, ACBD3 was located in the solution and PI is provided as micelles.	RESULTS
+124	126	PI	chemical	However, in vivo ACBD3 is located at the Golgi membranes, whereas in this experiment, ACBD3 was located in the solution and PI is provided as micelles.	RESULTS
+33	36	GUV	experimental_method	For this, we again turned to the GUV system with ACBD3 localized to the GUV membrane.	RESULTS
+49	54	ACBD3	protein	For this, we again turned to the GUV system with ACBD3 localized to the GUV membrane.	RESULTS
+55	64	localized	evidence	For this, we again turned to the GUV system with ACBD3 localized to the GUV membrane.	RESULTS
+72	75	GUV	experimental_method	For this, we again turned to the GUV system with ACBD3 localized to the GUV membrane.	RESULTS
+4	8	GUVs	experimental_method	The GUVs contained 10% PI to serve as a substrate for PI4KB kinase.	RESULTS
+23	25	PI	chemical	The GUVs contained 10% PI to serve as a substrate for PI4KB kinase.	RESULTS
+54	59	PI4KB	protein	The GUVs contained 10% PI to serve as a substrate for PI4KB kinase.	RESULTS
+60	66	kinase	protein_type	The GUVs contained 10% PI to serve as a substrate for PI4KB kinase.	RESULTS
+26	29	CFP	experimental_method	The buffer also contained CFP-SidC, which binds to PI4P with nanomolar affinity.	RESULTS
+30	34	SidC	protein	The buffer also contained CFP-SidC, which binds to PI4P with nanomolar affinity.	RESULTS
+51	55	PI4P	chemical	The buffer also contained CFP-SidC, which binds to PI4P with nanomolar affinity.	RESULTS
+34	40	kinase	protein_type	This enabled visualization of the kinase reaction using a confocal microscope.	RESULTS
+58	77	confocal microscope	experimental_method	This enabled visualization of the kinase reaction using a confocal microscope.	RESULTS
+34	49	phosphorylation	ptm	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
+66	72	kinase	protein_type	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
+73	78	alone	protein_state	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
+92	98	kinase	protein_type	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
+131	135	GUVs	experimental_method	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
+139	144	ACBD3	protein	We compared the efficiency of the phosphorylation reaction of the kinase alone with that of kinase recruited to the surface of the GUVs by ACBD3.	RESULTS
+35	45	absence of	protein_state	Reaction was also performed in the absence of ATP as a negative control (Fig. 4B).	RESULTS
+46	49	ATP	chemical	Reaction was also performed in the absence of ATP as a negative control (Fig. 4B).	RESULTS
+30	35	PI4KB	protein	These experiments showed that PI4KB enzymatic activity increases when ACBD3 is membrane localized (Fig. 4C, SI Fig. 6).	RESULTS
+36	54	enzymatic activity	evidence	These experiments showed that PI4KB enzymatic activity increases when ACBD3 is membrane localized (Fig. 4C, SI Fig. 6).	RESULTS
+70	75	ACBD3	protein	These experiments showed that PI4KB enzymatic activity increases when ACBD3 is membrane localized (Fig. 4C, SI Fig. 6).	RESULTS
+24	29	PI4KB	protein	Membrane recruitment of PI4KB enzyme is crucial to ensure its proper function at the Golgi and TGN.	DISCUSS
+58	63	PI4KB	protein	However, the molecular mechanism and structural basis for PI4KB interaction with the membrane is poorly understood.	DISCUSS
+45	50	PI4KB	protein	In principle, any of the binding partners of PI4KB could play a role in membrane recruitment.	DISCUSS
+17	22	PI4KB	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
+78	91	small GTPases	protein_type	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
+92	97	Rab11	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
+102	106	Arf1	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
+127	163	acyl-CoA binding domain containing 3	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
+165	170	ACBD3	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
+181	206	neuronal calcium sensor-1	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
+208	213	NCS-1	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
+228	237	frequenin	protein	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
+241	246	yeast	taxonomy_domain	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
+256	271	14-3-3 proteins	protein_type	To date, several PI4KB interacting proteins have been reported, including the small GTPases Rab11 and Arf1, the Golgi resident acyl-CoA binding domain containing 3 (ACBD3) protein, neuronal calcium sensor-1 (NCS-1 also known as frequenin in yeast) and the 14-3-3 proteins.	DISCUSS
+4	13	monomeric	oligomeric_state	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
+14	23	G protein	protein_type	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
+24	29	Rab11	protein	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
+36	45	mammalian	taxonomy_domain	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
+46	51	PI4KB	protein	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
+64	78	helical domain	structure_element	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
+86	92	kinase	protein_type	The monomeric G protein Rab11 binds mammalian PI4KB through the helical domain of the kinase.	DISCUSS
+9	14	Rab11	protein	Although Rab11 does not appear to be required for recruitment of PI4KB to the Golgi, PI4KB is required for Golgi recruitment of Rab11.	DISCUSS
+65	70	PI4KB	protein	Although Rab11 does not appear to be required for recruitment of PI4KB to the Golgi, PI4KB is required for Golgi recruitment of Rab11.	DISCUSS
+85	90	PI4KB	protein	Although Rab11 does not appear to be required for recruitment of PI4KB to the Golgi, PI4KB is required for Golgi recruitment of Rab11.	DISCUSS
+128	133	Rab11	protein	Although Rab11 does not appear to be required for recruitment of PI4KB to the Golgi, PI4KB is required for Golgi recruitment of Rab11.	DISCUSS
+0	4	Arf1	protein	Arf1, the other small GTP binding protein, is known to influence the activity and localization of PI4KB, but it does not appear to interact directly with PI4KB (our unpublished data).	DISCUSS
+16	41	small GTP binding protein	protein_type	Arf1, the other small GTP binding protein, is known to influence the activity and localization of PI4KB, but it does not appear to interact directly with PI4KB (our unpublished data).	DISCUSS
+98	103	PI4KB	protein	Arf1, the other small GTP binding protein, is known to influence the activity and localization of PI4KB, but it does not appear to interact directly with PI4KB (our unpublished data).	DISCUSS
+154	159	PI4KB	protein	Arf1, the other small GTP binding protein, is known to influence the activity and localization of PI4KB, but it does not appear to interact directly with PI4KB (our unpublished data).	DISCUSS
+4	9	yeast	taxonomy_domain	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
+23	27	NCS1	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
+35	44	frequenin	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
+77	82	Pik1p	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
+88	93	yeast	taxonomy_domain	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
+108	113	PI4KB	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
+194	199	NCS-1	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
+203	208	PI4KB	protein	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
+224	233	mammalian	taxonomy_domain	The yeast homologue of NCS1 called frequenin has been shown to interact with Pik1p, the yeast orthologue of PI4KB and regulate its activity and perhaps its membrane association, but the role of NCS-1 in PI4KB recruitment in mammalian cells is unclear.	DISCUSS
+0	5	NCS-1	protein	NCS-1 is an N-terminally myristoylated protein that participates in exocytosis.	DISCUSS
+25	38	myristoylated	protein_state	NCS-1 is an N-terminally myristoylated protein that participates in exocytosis.	DISCUSS
+81	86	PI4KB	protein	It is expressed only in certain cell types, suggesting that if it contributes to PI4KB membrane recruitment, it does so in a tissues specific manner.	DISCUSS
+19	24	PI4KB	protein	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
+30	45	14-3-3 proteins	protein_type	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
+59	74	phosphorylation	ptm	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
+78	83	PI4KB	protein	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
+87	103	protein kinase D	protein	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
+132	137	PI4KB	protein	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
+157	163	active	protein_state	The interaction of PI4KB with 14-3-3 proteins, promoted by phosphorylation of PI4KB by protein kinase D, influences the activity of PI4KB by stabilizing its active conformation.	DISCUSS
+9	24	14-3-3 proteins	protein_type	However, 14-3-3 proteins do not appear to interfere with membrane recruitment of this kinase.	DISCUSS
+86	92	kinase	protein_type	However, 14-3-3 proteins do not appear to interfere with membrane recruitment of this kinase.	DISCUSS
+0	5	ACBD3	protein	ACBD3 is a Golgi resident protein, conserved among vertebrates (SI Fig. 7), that interacts directly with PI4KB (see also SI Fig. 8 and SI Discussion), and whose genetic inactivation interferes with the Golgi localization of the kinase.	DISCUSS
+35	44	conserved	protein_state	ACBD3 is a Golgi resident protein, conserved among vertebrates (SI Fig. 7), that interacts directly with PI4KB (see also SI Fig. 8 and SI Discussion), and whose genetic inactivation interferes with the Golgi localization of the kinase.	DISCUSS
+51	62	vertebrates	taxonomy_domain	ACBD3 is a Golgi resident protein, conserved among vertebrates (SI Fig. 7), that interacts directly with PI4KB (see also SI Fig. 8 and SI Discussion), and whose genetic inactivation interferes with the Golgi localization of the kinase.	DISCUSS
+105	110	PI4KB	protein	ACBD3 is a Golgi resident protein, conserved among vertebrates (SI Fig. 7), that interacts directly with PI4KB (see also SI Fig. 8 and SI Discussion), and whose genetic inactivation interferes with the Golgi localization of the kinase.	DISCUSS
+228	234	kinase	protein_type	ACBD3 is a Golgi resident protein, conserved among vertebrates (SI Fig. 7), that interacts directly with PI4KB (see also SI Fig. 8 and SI Discussion), and whose genetic inactivation interferes with the Golgi localization of the kinase.	DISCUSS
+55	60	PI4KB	protein	For these reasons we focused on the interaction of the PI4KB enzyme with the Golgi resident ACBD3 protein in this study.	DISCUSS
+92	97	ACBD3	protein	For these reasons we focused on the interaction of the PI4KB enzyme with the Golgi resident ACBD3 protein in this study.	DISCUSS
+58	63	PI4KB	protein	Here we present the mechanism for membrane recruitment of PI4KB by the Golgi resident ACBD3 protein.	DISCUSS
+86	91	ACBD3	protein	Here we present the mechanism for membrane recruitment of PI4KB by the Golgi resident ACBD3 protein.	DISCUSS
+53	55	Kd	evidence	We show that these proteins interact directly with a Kd value in the submicromolar range.	DISCUSS
+41	46	PI4KB	protein	The interaction is sufficient to recruit PI4KB to model membranes in vitro as well as to the mitochondria where PI4KB is never naturally found.	DISCUSS
+112	117	PI4KB	protein	The interaction is sufficient to recruit PI4KB to model membranes in vitro as well as to the mitochondria where PI4KB is never naturally found.	DISCUSS
+50	56	solved	experimental_method	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
+61	79	solution structure	evidence	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
+83	94	ACBD3:PI4KB	complex_assembly	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
+136	141	PI4KB	protein	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
+142	159	N-terminal region	structure_element	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
+171	193	short amphipatic helix	structure_element	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
+204	209	44–64	residue_range	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
+226	231	ACBD3	protein	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
+232	240	Q domain	structure_element	To understand this process at the atomic level we solved the solution structure of ACBD3:PI4KB sub complex (Fig. 1A) and found that the PI4KB N-terminal region contains a short amphipatic helix (residues 44–64) that binds the ACBD3 Q domain.	DISCUSS
+4	12	Q domain	structure_element	The Q domain adopts a helical hairpin fold that is further stabilized upon binding the kinase helix (Fig. 2A).	DISCUSS
+22	42	helical hairpin fold	structure_element	The Q domain adopts a helical hairpin fold that is further stabilized upon binding the kinase helix (Fig. 2A).	DISCUSS
+87	99	kinase helix	structure_element	The Q domain adopts a helical hairpin fold that is further stabilized upon binding the kinase helix (Fig. 2A).	DISCUSS
+115	121	kinase	protein_type	Our data strongly suggest that formation of the complex does not directly influence the catalytic abilities of the kinase but experiments with model membranes revealed that ACBD3 enhances catalytic activity of the kinase by a recruitment based mechanism; it recruits the kinase to the membrane and thus increases the local concentration of the substrate in the vicinity of the kinase.	DISCUSS
+173	178	ACBD3	protein	Our data strongly suggest that formation of the complex does not directly influence the catalytic abilities of the kinase but experiments with model membranes revealed that ACBD3 enhances catalytic activity of the kinase by a recruitment based mechanism; it recruits the kinase to the membrane and thus increases the local concentration of the substrate in the vicinity of the kinase.	DISCUSS
+214	220	kinase	protein_type	Our data strongly suggest that formation of the complex does not directly influence the catalytic abilities of the kinase but experiments with model membranes revealed that ACBD3 enhances catalytic activity of the kinase by a recruitment based mechanism; it recruits the kinase to the membrane and thus increases the local concentration of the substrate in the vicinity of the kinase.	DISCUSS
+271	277	kinase	protein_type	Our data strongly suggest that formation of the complex does not directly influence the catalytic abilities of the kinase but experiments with model membranes revealed that ACBD3 enhances catalytic activity of the kinase by a recruitment based mechanism; it recruits the kinase to the membrane and thus increases the local concentration of the substrate in the vicinity of the kinase.	DISCUSS
+377	383	kinase	protein_type	Our data strongly suggest that formation of the complex does not directly influence the catalytic abilities of the kinase but experiments with model membranes revealed that ACBD3 enhances catalytic activity of the kinase by a recruitment based mechanism; it recruits the kinase to the membrane and thus increases the local concentration of the substrate in the vicinity of the kinase.	DISCUSS
+38	48	structures	evidence	Based on our and previously published structures we built a pseudoatomic model of PI4KB multi-protein assembly on the membrane (Fig. 5) that illustrates how the enzyme is recruited and positioned towards its lipidic substrate and how it in turn recruits Rab11.	DISCUSS
+60	78	pseudoatomic model	evidence	Based on our and previously published structures we built a pseudoatomic model of PI4KB multi-protein assembly on the membrane (Fig. 5) that illustrates how the enzyme is recruited and positioned towards its lipidic substrate and how it in turn recruits Rab11.	DISCUSS
+82	87	PI4KB	protein	Based on our and previously published structures we built a pseudoatomic model of PI4KB multi-protein assembly on the membrane (Fig. 5) that illustrates how the enzyme is recruited and positioned towards its lipidic substrate and how it in turn recruits Rab11.	DISCUSS
+254	259	Rab11	protein	Based on our and previously published structures we built a pseudoatomic model of PI4KB multi-protein assembly on the membrane (Fig. 5) that illustrates how the enzyme is recruited and positioned towards its lipidic substrate and how it in turn recruits Rab11.	DISCUSS
+0	12	+RNA viruses	taxonomy_domain	+RNA viruses replicate at specific PI4P-enriched membranous compartments.	DISCUSS
+35	39	PI4P	chemical	+RNA viruses replicate at specific PI4P-enriched membranous compartments.	DISCUSS
+61	66	viral	taxonomy_domain	These are called replication factories (because they enhance viral replication) or membranous webs (because of their appearance under the electron microscope).	DISCUSS
+35	42	viruses	taxonomy_domain	To generate replication factories, viruses hijack several host factors including the PI4K kinases to secure high content of the PI4P lipid.	DISCUSS
+85	89	PI4K	protein_type	To generate replication factories, viruses hijack several host factors including the PI4K kinases to secure high content of the PI4P lipid.	DISCUSS
+90	97	kinases	protein_type	To generate replication factories, viruses hijack several host factors including the PI4K kinases to secure high content of the PI4P lipid.	DISCUSS
+128	132	PI4P	chemical	To generate replication factories, viruses hijack several host factors including the PI4K kinases to secure high content of the PI4P lipid.	DISCUSS
+133	138	lipid	chemical	To generate replication factories, viruses hijack several host factors including the PI4K kinases to secure high content of the PI4P lipid.	DISCUSS
+0	26	Non-structural 3A proteins	protein_type	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
+37	51	picornaviruses	taxonomy_domain	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
+61	72	Enterovirus	taxonomy_domain	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
+79	89	poliovirus	species	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
+91	108	coxsackievirus-B3	species	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
+110	123	rhinovirus-14	species	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
+129	138	Kobuvirus	taxonomy_domain	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
+145	158	Aichi virus-1	species	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
+190	195	ACBD3	protein	Non-structural 3A proteins from many picornaviruses from the Enterovirus (e.g. poliovirus, coxsackievirus-B3, rhinovirus-14) and Kobuvirus (e.g. Aichi virus-1) genera directly interact with ACBD3.	DISCUSS
+45	59	3A:ACBD3:PI4KB	complex_assembly	Our data suggest that they could do this via 3A:ACBD3:PI4KB complex formation.	DISCUSS
+4	13	structure	evidence	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
+21	26	ACBD3	protein	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
+27	35	Q domain	structure_element	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
+44	56	kinase helix	structure_element	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
+137	142	ACBD3	protein	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
+144	149	PI4KB	protein	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
+159	170	ACBD3:PI4KB	complex_assembly	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
+186	198	picornaviral	taxonomy_domain	The structure of the ACBD3 Q domain and the kinase helix described here provides a novel opportunity for further research on the role of ACBD3, PI4KB, and the ACBD3:PI4KB interaction in picornaviral replication.	DISCUSS
+79	93	picornaviruses	taxonomy_domain	This could eventually have implications for therapeutic intervention to combat picornaviruses-mediated diseases ranging from polio to the common cold.	DISCUSS
+0	28	Biochemical characterization	experimental_method	Biochemical characterization of the ACBD3:PI4KB complex.	FIG
+36	47	ACBD3:PI4KB	complex_assembly	Biochemical characterization of the ACBD3:PI4KB complex.	FIG
+36	41	ACBD3	protein	(A) Schematic representation of the ACBD3 and PI4KB constructs used for the experiments.	FIG
+46	51	PI4KB	protein	(A) Schematic representation of the ACBD3 and PI4KB constructs used for the experiments.	FIG
+0	5	ACBD3	protein	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
+19	42	acyl-CoA binding domain	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
+44	48	ACBD	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
+51	77	charged amino acids region	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
+79	82	CAR	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
+85	106	glutamine rich region	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
+108	109	Q	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
+116	137	Golgi dynamics domain	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
+139	143	GOLD	structure_element	ACBD3 contains the acyl-CoA binding domain (ACBD), charged amino acids region (CAR), glutamine rich region (Q), and Golgi dynamics domain (GOLD).	FIG
+0	5	PI4KB	protein	PI4KB is composed of the N-terminal region, helical domain, and kinase domain which can be divided into N- and C-terminal lobes.	FIG
+25	42	N-terminal region	structure_element	PI4KB is composed of the N-terminal region, helical domain, and kinase domain which can be divided into N- and C-terminal lobes.	FIG
+44	58	helical domain	structure_element	PI4KB is composed of the N-terminal region, helical domain, and kinase domain which can be divided into N- and C-terminal lobes.	FIG
+64	77	kinase domain	structure_element	PI4KB is composed of the N-terminal region, helical domain, and kinase domain which can be divided into N- and C-terminal lobes.	FIG
+104	127	N- and C-terminal lobes	structure_element	PI4KB is composed of the N-terminal region, helical domain, and kinase domain which can be divided into N- and C-terminal lobes.	FIG
+4	28	In vitro pull-down assay	experimental_method	(B) In vitro pull-down assay.	FIG
+0	16	Pull-down assays	experimental_method	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
+67	81	His6GB1-tagged	protein_state	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
+108	116	untagged	protein_state	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
+117	128	full-length	protein_state	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
+129	134	PI4KB	protein	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
+138	143	ACBD3	protein	Pull-down assays were performed using NiNTA-immobilized N-terminal His6GB1-tagged proteins as indicated and untagged full-length PI4KB or ACBD3.	FIG
+47	55	SDS gels	experimental_method	The inputs and bound proteins were analyzed on SDS gels stained with Coomassie Blue.	FIG
+35	46	full-length	protein_state	Please, see SI Fig. 9 for original full-length gels. (C) Analytical Ultracentrifugation.	FIG
+57	87	Analytical Ultracentrifugation	experimental_method	Please, see SI Fig. 9 for original full-length gels. (C) Analytical Ultracentrifugation.	FIG
+0	3	AUC	experimental_method	AUC analysis of the ACBD3:PI4KB full-length complex at the concentration of 5 μM (both proteins, left panel) and ACBD3 Q domain: PI4KB N terminal region complex at the concentration of 35 μM (both proteins, right panel). (D) Surface plasmon resonance.	FIG
+20	31	ACBD3:PI4KB	complex_assembly	AUC analysis of the ACBD3:PI4KB full-length complex at the concentration of 5 μM (both proteins, left panel) and ACBD3 Q domain: PI4KB N terminal region complex at the concentration of 35 μM (both proteins, right panel). (D) Surface plasmon resonance.	FIG
+32	43	full-length	protein_state	AUC analysis of the ACBD3:PI4KB full-length complex at the concentration of 5 μM (both proteins, left panel) and ACBD3 Q domain: PI4KB N terminal region complex at the concentration of 35 μM (both proteins, right panel). (D) Surface plasmon resonance.	FIG
+113	152	ACBD3 Q domain: PI4KB N terminal region	complex_assembly	AUC analysis of the ACBD3:PI4KB full-length complex at the concentration of 5 μM (both proteins, left panel) and ACBD3 Q domain: PI4KB N terminal region complex at the concentration of 35 μM (both proteins, right panel). (D) Surface plasmon resonance.	FIG
+225	250	Surface plasmon resonance	experimental_method	AUC analysis of the ACBD3:PI4KB full-length complex at the concentration of 5 μM (both proteins, left panel) and ACBD3 Q domain: PI4KB N terminal region complex at the concentration of 35 μM (both proteins, right panel). (D) Surface plasmon resonance.	FIG
+0	3	SPR	experimental_method	SPR analysis of the PI4KB binding to immobilized ACBD3.	FIG
+20	25	PI4KB	protein	SPR analysis of the PI4KB binding to immobilized ACBD3.	FIG
+49	54	ACBD3	protein	SPR analysis of the PI4KB binding to immobilized ACBD3.	FIG
+0	11	Sensorgrams	evidence	Sensorgrams for four concentrations of PI4KB are shown.	FIG
+39	44	PI4KB	protein	Sensorgrams for four concentrations of PI4KB are shown.	FIG
+0	19	Structural analysis	experimental_method	Structural analysis of the ACBD3:PI4KB complex.	FIG
+27	38	ACBD3:PI4KB	complex_assembly	Structural analysis of the ACBD3:PI4KB complex.	FIG
+12	21	structure	evidence	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
+29	34	ACBD3	protein	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
+35	43	Q domain	structure_element	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
+58	73	in complex with	protein_state	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
+78	83	PI4KB	protein	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
+84	101	N-terminal region	structure_element	(A) Overall structure of the ACBD3 Q domain by itself and in complex with the PI4KB N-terminal region.	FIG
+0	13	Superposition	experimental_method	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
+34	44	structures	evidence	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
+62	70	Q domain	structure_element	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
+98	108	structures	evidence	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
+158	164	folded	protein_state	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
+173	178	PI4KB	protein	Superposition of the 30 converged structures obtained for the Q domain (top) and the 45 converged structures obtained for the complex (bottom), with only the folded part of PI4KB shown (see SI Fig. 2 for the complete view). (B) Detailed view of the complex.	FIG
+43	57	hydrogen bonds	bond_interaction	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+59	64	ACBD3	protein	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+65	71	Tyr261	residue_name_number	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+73	78	PI4KB	protein	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+79	84	His63	residue_name_number	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+89	94	ACBD3	protein	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+95	101	Tyr288	residue_name_number	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+103	108	PI4KB	protein	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+109	114	Asp44	residue_name_number	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+127	146	hydrophobic surface	site	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+154	166	kinase helix	structure_element	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+180	185	ACBD3	protein	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+186	194	Q domain	structure_element	The interaction is facilitated by only two hydrogen bonds (ACBD3 Tyr261: PI4KB His63 and ACBD3 Tyr288: PI4KB Asp44), while the hydrophobic surface of the kinase helix nests in the ACBD3 Q domain.	FIG
+0	5	ACBD3	protein	ACBD3 is shown in magenta and PI4KB in orange.	FIG
+30	35	PI4KB	protein	ACBD3 is shown in magenta and PI4KB in orange.	FIG
+20	32	kinase helix	structure_element	(C) Top view of the kinase helix.	FIG
+4	16	kinase helix	structure_element	The kinase helix is amphipathic and its hydrophobic surface overlaps with the ACBD3 binding surface (shown in magenta).	FIG
+20	31	amphipathic	protein_state	The kinase helix is amphipathic and its hydrophobic surface overlaps with the ACBD3 binding surface (shown in magenta).	FIG
+40	59	hydrophobic surface	site	The kinase helix is amphipathic and its hydrophobic surface overlaps with the ACBD3 binding surface (shown in magenta).	FIG
+78	83	ACBD3	protein	The kinase helix is amphipathic and its hydrophobic surface overlaps with the ACBD3 binding surface (shown in magenta).	FIG
+84	99	binding surface	site	The kinase helix is amphipathic and its hydrophobic surface overlaps with the ACBD3 binding surface (shown in magenta).	FIG
+160	175	Pull-down assay	experimental_method	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
+214	228	His6GB1-tagged	protein_state	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
+229	234	PI4KB	protein	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
+235	241	kinase	protein_type	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
+246	254	untagged	protein_state	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
+255	260	ACBD3	protein	Strong and weak hydrophobes are in green and cyan respectively, basic residues in blue, acidic residues in red and nonpolar hydrophilic residues in orange. (D) Pull-down assay with a NiNTA-immobilized N-terminally His6GB1-tagged PI4KB kinase and untagged ACBD3 protein.	FIG
+0	9	Wild type	protein_state	Wild type proteins and selected point mutants of both PI4KB and ACBD3 were used.	FIG
+38	45	mutants	protein_state	Wild type proteins and selected point mutants of both PI4KB and ACBD3 were used.	FIG
+54	59	PI4KB	protein	Wild type proteins and selected point mutants of both PI4KB and ACBD3 were used.	FIG
+64	69	ACBD3	protein	Wild type proteins and selected point mutants of both PI4KB and ACBD3 were used.	FIG
+35	46	full-length	protein_state	Please, see SI Fig. 9 for original full-length gels.	FIG
+0	5	ACBD3	protein	ACBD3 is sufficient to recruit the PI4KB kinase to membranes.	FIG
+35	40	PI4KB	protein	ACBD3 is sufficient to recruit the PI4KB kinase to membranes.	FIG
+41	47	kinase	protein_type	ACBD3 is sufficient to recruit the PI4KB kinase to membranes.	FIG
+4	26	GUVs recruitment assay	experimental_method	(A) GUVs recruitment assay.	FIG
+34	40	kinase	protein_type	Top – Virtually no membrane bound kinase was observed when 600 nM PI4KB was added to the GUVs.	FIG
+66	71	PI4KB	protein	Top – Virtually no membrane bound kinase was observed when 600 nM PI4KB was added to the GUVs.	FIG
+89	93	GUVs	experimental_method	Top – Virtually no membrane bound kinase was observed when 600 nM PI4KB was added to the GUVs.	FIG
+16	27	presence of	protein_state	Bottom – in the presence of 600 nM GUV tethered ACBD3 a significant signal of the kinase is detected on the surface of GUVs.	FIG
+35	47	GUV tethered	protein_state	Bottom – in the presence of 600 nM GUV tethered ACBD3 a significant signal of the kinase is detected on the surface of GUVs.	FIG
+48	53	ACBD3	protein	Bottom – in the presence of 600 nM GUV tethered ACBD3 a significant signal of the kinase is detected on the surface of GUVs.	FIG
+82	88	kinase	protein_type	Bottom – in the presence of 600 nM GUV tethered ACBD3 a significant signal of the kinase is detected on the surface of GUVs.	FIG
+119	123	GUVs	experimental_method	Bottom – in the presence of 600 nM GUV tethered ACBD3 a significant signal of the kinase is detected on the surface of GUVs.	FIG
+4	33	Golgi displacement experiment	experimental_method	(B) Golgi displacement experiment.	FIG
+13	18	ACBD3	protein	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
+19	27	Q domain	structure_element	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
+37	40	GFP	experimental_method	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
+45	58	overexpressed	experimental_method	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
+78	83	PI4KB	protein	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
+88	101	immunostained	experimental_method	Upper panel: ACBD3 Q domain fused to GFP was overexpressed and the endogenous PI4KB was immunostained.	FIG
+49	52	GFP	experimental_method	Middle panel: The same experiment performed with GFP alone.	FIG
+48	54	mutant	protein_state	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+55	63	Q domain	structure_element	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+65	70	F258A	mutant	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+72	77	H284A	mutant	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+79	84	Y288A	mutant	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+109	114	PI4KB	protein	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+120	125	ACBD3	protein	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+126	134	Q domain	structure_element	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+135	149	overexpression	experimental_method	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+159	167	ceramide	chemical	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+218	227	wild-type	protein_state	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+228	233	ACBD3	protein	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+234	242	Q domain	structure_element	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+243	247	FKBP	protein	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+248	252	mRFP	experimental_method	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+278	296	Bodipy FL-Ceramide	chemical	Lower panel: The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (C) ACBD3 Q domain overexpression inhibits ceramide transport to Golgi – COS-7 cells transfected with wild-type ACBD3 Q domain-FKBP-mRFP were loaded with 0.05 μM Bodipy FL-Ceramide for 20 min, then washed and depicted after 20 min.	FIG
+50	54	mRFP	experimental_method	Middle panel – The same experiment performed with mRFP-FKBP alone.	FIG
+55	59	FKBP	protein	Middle panel – The same experiment performed with mRFP-FKBP alone.	FIG
+49	55	mutant	protein_state	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
+56	64	Q domain	structure_element	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
+66	71	F258A	mutant	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
+73	78	H284A	mutant	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
+80	85	Y288A	mutant	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
+110	115	PI4KB	protein	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
+135	170	mitochondria recruitment experiment	experimental_method	Lower panel – The same experiment performed with mutant Q domain (F258A, H284A, Y288A) that does not bind the PI4KB. (D) Scheme of the mitochondria recruitment experiment.	FIG
+6	11	AKAP1	protein	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
+12	15	FRB	structure_element	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
+16	19	CFP	experimental_method	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
+33	42	localized	evidence	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
+90	93	GFP	experimental_method	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
+94	99	PI4KB	protein	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
+104	112	Q domain	structure_element	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
+113	117	FKBP	protein	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
+118	122	mRFP	experimental_method	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
+138	147	localized	evidence	– The AKAP1-FRB-CFP construct is localized at the outer mitochondrial membrane, while the GFP-PI4KB and Q domain-FKBP-mRFP constructs are localized in the cytoplasm where they can form a complex.	FIG
+17	26	rapamycin	chemical	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
+31	39	Q domain	structure_element	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
+40	44	FKBP	protein	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
+45	49	mRFP	experimental_method	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
+103	106	GFP	experimental_method	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
+107	112	PI4KB	protein	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
+126	161	Mitochondria recruitment experiment	experimental_method	Upon addition of rapamycin the Q domain-FKBP-mRFP construct translocates to the mitochondria and takes GFP-PI4KB with it. (E) Mitochondria recruitment experiment.	FIG
+30	35	AKAP1	protein	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
+36	39	FRB	structure_element	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
+40	43	CFP	experimental_method	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
+45	48	GFP	experimental_method	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
+49	54	PI4KB	protein	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
+59	68	wild-type	protein_state	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
+69	77	Q domain	structure_element	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
+78	82	FKBP	protein	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
+83	87	mRFP	experimental_method	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
+141	150	rapamycin	chemical	Left – cells transfected with AKAP1-FRB-CFP, GFP-PI4KB and wild-type Q domain-FKBP-mRFP constructs before and five minutes after addition of rapamycin.	FIG
+48	53	H264A	mutant	Right – The same experiment performed using the H264A Q domain mutant.	FIG
+54	62	Q domain	structure_element	Right – The same experiment performed using the H264A Q domain mutant.	FIG
+63	69	mutant	protein_state	Right – The same experiment performed using the H264A Q domain mutant.	FIG
+0	5	ACBD3	protein	ACBD3 indirectly increases the activity of PI4KB.	FIG
+43	48	PI4KB	protein	ACBD3 indirectly increases the activity of PI4KB.	FIG
+4	31	Micelles-based kinase assay	experimental_method	(A) Micelles-based kinase assay – PI in TX100 micelles was used in a luminescent kinase assay and the production of PI4P was measured.	FIG
+34	36	PI	chemical	(A) Micelles-based kinase assay – PI in TX100 micelles was used in a luminescent kinase assay and the production of PI4P was measured.	FIG
+69	93	luminescent kinase assay	experimental_method	(A) Micelles-based kinase assay – PI in TX100 micelles was used in a luminescent kinase assay and the production of PI4P was measured.	FIG
+116	120	PI4P	chemical	(A) Micelles-based kinase assay – PI in TX100 micelles was used in a luminescent kinase assay and the production of PI4P was measured.	FIG
+38	42	PI4P	chemical	Bar graph presents the mean values of PI4P generated in the presence of the proteins as indicated, normalized to the amount of PI4P generated by PI4KB alone.	FIG
+60	71	presence of	protein_state	Bar graph presents the mean values of PI4P generated in the presence of the proteins as indicated, normalized to the amount of PI4P generated by PI4KB alone.	FIG
+127	131	PI4P	chemical	Bar graph presents the mean values of PI4P generated in the presence of the proteins as indicated, normalized to the amount of PI4P generated by PI4KB alone.	FIG
+145	150	PI4KB	protein	Bar graph presents the mean values of PI4P generated in the presence of the proteins as indicated, normalized to the amount of PI4P generated by PI4KB alone.	FIG
+15	42	standard errors of the mean	evidence	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
+44	47	SEM	evidence	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
+93	124	GUV-based phosphorylation assay	experimental_method	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
+127	131	GUVs	experimental_method	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
+147	149	PI	chemical	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
+197	201	PI4P	chemical	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
+225	243	CFP-SidC biosensor	experimental_method	Error bars are standard errors of the mean (SEM) based on three independent experiments. (B) GUV-based phosphorylation assay – GUVs containing 10% PI were used as a substrate and the production of PI4P was measured using the CFP-SidC biosensor.	FIG
+26	51	GUV phosphorylation assay	experimental_method	(C)–Quantification of the GUV phosphorylation assay – Mean membrane fluorescence intensity of the PI4P reporter (SidC-label) under different protein/ATP conditions.	FIG
+54	90	Mean membrane fluorescence intensity	evidence	(C)–Quantification of the GUV phosphorylation assay – Mean membrane fluorescence intensity of the PI4P reporter (SidC-label) under different protein/ATP conditions.	FIG
+98	102	PI4P	chemical	(C)–Quantification of the GUV phosphorylation assay – Mean membrane fluorescence intensity of the PI4P reporter (SidC-label) under different protein/ATP conditions.	FIG
+113	117	SidC	protein	(C)–Quantification of the GUV phosphorylation assay – Mean membrane fluorescence intensity of the PI4P reporter (SidC-label) under different protein/ATP conditions.	FIG
+149	152	ATP	chemical	(C)–Quantification of the GUV phosphorylation assay – Mean membrane fluorescence intensity of the PI4P reporter (SidC-label) under different protein/ATP conditions.	FIG
+4	27	mean membrane intensity	evidence	The mean membrane intensity value is relative to the background signal and the difference between the membrane and background signal in the reference system lacking ATP.	FIG
+165	168	ATP	chemical	The mean membrane intensity value is relative to the background signal and the difference between the membrane and background signal in the reference system lacking ATP.	FIG
+25	28	SEM	evidence	The error bars stand for SEM based on three independent experiments (also SI Fig. 6).	FIG
+0	18	Pseudoatomic model	evidence	Pseudoatomic model of the PI4KB multiprotein complex assembly.	FIG
+26	31	PI4KB	protein	Pseudoatomic model of the PI4KB multiprotein complex assembly.	FIG
+0	5	PI4KB	protein	PI4KB in orange, Rab11 in purple, ACBD3 in blue.	FIG
+17	22	Rab11	protein	PI4KB in orange, Rab11 in purple, ACBD3 in blue.	FIG
+34	39	ACBD3	protein	PI4KB in orange, Rab11 in purple, ACBD3 in blue.	FIG
+26	29	NMR	experimental_method	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
+30	39	structure	evidence	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
+67	84	crystal structure	evidence	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
+88	99	PI4KB:Rab11	complex_assembly	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
+125	129	ACBD	structure_element	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
+134	138	GOLD	structure_element	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
+151	167	homology modeled	experimental_method	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
+200	210	structures	evidence	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
+227	233	Phyre2	experimental_method	The model is based on our NMR structure and a previously published crystal structure of PI4KB:Rab11 complex (PDB code 4D0L), ACBD and GOLD domain were homology modeled based on high sequence identity structures produced by the Phyre2 web server.	FIG
+4	8	GOLD	structure_element	The GOLD domain is tethered to the membrane by GolginB1 (also known as Giantin) which is not shown for clarity.	FIG
+47	55	GolginB1	protein	The GOLD domain is tethered to the membrane by GolginB1 (also known as Giantin) which is not shown for clarity.	FIG
+71	78	Giantin	protein	The GOLD domain is tethered to the membrane by GolginB1 (also known as Giantin) which is not shown for clarity.	FIG
+0	32	Intrinsically disordered linkers	structure_element	Intrinsically disordered linkers are modeled in an arbitrary but physically plausible conformation.	FIG