GPCR Signalling Complexes – Synthesis, Assembly, Trafficking and Specificity [electronic resource] /
Dupré, Denis J.editor.
Hébert, Terence E.editor.
Jockers, Ralf.editor.
This book provides a broad survey of various topics pertaining to G protein coupled receptor (GPCR) assembly into specific signalling complexes, and the regulation of the events leading to this assembly. Throughout this book, we focus on one main area: GPCRs are involved in highly efficient and specific activation of signalling pathways; how are these signalling complexes assembled to generate such specificity? To address this issue, we need to understand how receptors and their signalling partners are synthesized, folded correctly and assembled in order to generate functional complexes. The effects of oligomerization on specificity and efficacy of signal transduction are also discussed. Once receptor complexes are assembled, how are they targeted to different intracellular sites and what controls the trafficking of GPCR signalling complexes? Finally, defects in synthesis, maturation or trafficking can alter functionality of GPCR signalling complexes; how can we manipulate these systems to normalize them functionally?  Therefore, the topics to be covered in this book are: 1) Molecular chaperones involved in regulating (quality control) of GPCR synthesis; 2) Assembly of signalling complexes, or subunits of the complex and their organization; 3) GPCR oligomerization; 4) GPCR trafficking; 5) Problems of trafficking: pharmacological chaperones to the rescue.
""GPCR Signalling Complexes â€? Synthesis, Assembly, Trafficking and Specificity""; ""Contents""; ""Introduction""; ""Chapter 1: ER-Bound Steps in the Biosynthesis of G Protein-Coupled Receptors""; ""1.1 Membrane Insertion of the Receptor Polypeptide""; ""1.1.1 Membrane Insertion in the Presence or Absence of a Signal Peptide""; ""1.1.2 Additional Functions of Signal Peptides""; ""1.1.3 Glycosylation""; ""1.2 Stability of the Receptor Structure""; ""1.3 The Transmembrane Domain""; ""1.4 The Extracellular Domain""; ""1.5 Helix Eight of the Cytoplasmic Domain""; ""1.5.1 ER Quality Control""
""1.6 ERAD (Endoplasmic Reticulum Associated Degradation)""""1.7 G Protein-Coupled Receptors Interacting with Chaperone Molecules""; ""1.8 A Consideration Regarding the Experimental Assessment of ER Quality Control in Mammalian Cells""; ""References""; ""Chapter 2: Role of Chaperones in G Protein Coupled Receptor Signaling Complex Assembly""; ""2.1 Introduction""; ""2.2 GPCR Dimerization""; ""2.3 Receptor Maturation""; ""2.4 Molecular Chaperones""; ""2.5 Molecular Chaperones and GPCRs""; ""2.6 Signaling Complex Assembly""; ""2.7 Conclusion""; ""References""
""Chapter 3: GPCR Oligomerization: Contribution to Receptor Biogenesis""""3.1 Introduction""; ""3.2 How to Study Oligomerization During Biogenesis""; ""3.2.1 Co-immunoprecipitation""; ""3.2.2 Biophysical Methods""; ""3.2.2.1 Fluorescence Resonance Energy Transfer Techniques (FRET)""; "" Classic FRET Approach""; "" New Advances of FRET""; ""3.2.2.2 Bioluminescence Resonance Energy Transfer Techniques (BRET)""; ""3.2.2.3 Bimolecular Fluorescence or Luminescence Complementation (BiFC/BiLC)""; ""3.2.3 Proximity Ligation Assay (PLA)""
""3.2.4 The Use of Mutants: Dominant Negative and ER Trapping Studies""""3.3 Folding of GPCRs""; ""3.3.1 Translation of GPCR mRNA""; ""3.3.2 Receptor Biogenesis in the Endoplasmic Reticulum""; ""3.4 Exit from the ER and Trafficking to the Plasma Membrane""; ""3.5 Functionality of GPCRs at the Plasma Membrane""; ""3.6 Role of Dimerization in the Biogenesis of Different GPCR Family Members""; ""3.6.1 Family A""; ""3.6.2 Family B""; ""3.6.3 Family C""; ""3.7 Receptor-Receptor Interaction Domains: The GPCR as a Chaperone, Promoting Folding""
""3.8 How Biogenesis of GPCR Oligomers can be Influenced""""3.8.1 Role of the Availability of Different GPCRs""; ""3.8.2 Availability of GPCR Ligands""; ""3.9 Concluding Remarks""; ""References""; ""Chapter 4: The Functional Size of GPCRs â€? Monomers, Dimers or Tetramers?""; ""4.1 Introduction""; ""4.2 What Crystal Structures Tell us About GPCR Dimers""; ""4.3 Î²AR Homodimers""; ""4.4 Î²AR Heterodimerization â€? Family Gatherings""; ""4.5 Î²AR Heterodimerization â€? Extending the GPCR Interactome""; ""4.6 Î²AR Interactions with Other Receptor Classes""; ""4.7 Monomer: Dimer Equilibria""
""4.8 Larger Arrays of GPCRs?""
Includes index.
This book provides a broad survey of various topics pertaining to G protein coupled receptor (GPCR) assembly into specific signalling complexes, and the regulation of the events leading to this assembly. Throughout this book, we focus on one main area: GPCRs are involved in highly efficient and specific activation of signalling pathways; how are these signalling complexes assembled to generate such specificity? To address this issue, we need to understand how receptors and their signalling partners are synthesized, folded correctly and assembled in order to generate functional complexes. The effects of oligomerization on specificity and efficacy of signal transduction are also discussed. Once receptor complexes are assembled, how are they targeted to different intracellular sites and what controls the trafficking of GPCR signalling complexes? Finally, defects in synthesis, maturation or trafficking can alter functionality of GPCR signalling complexes; how can we manipulate these systems to normalize them functionally?  Therefore, the topics to be covered in this book are: 1) Molecular chaperones involved in regulating (quality control) of GPCR synthesis; 2) Assembly of signalling complexes, or subunits of the complex and their organization; 3) GPCR oligomerization; 4) GPCR trafficking; 5) Problems of trafficking: pharmacological chaperones to the rescue.
Medicine.
Pharmacology.
Proteins .
Medical biochemistry.
Biomedicine, general.
Pharmacology/Toxicology.
Receptors.
Medical Biochemistry.


Subcellular Biochemistry