EMBO/soda-nel huggingface dataset:
ABCA12 regulates insulin secretion from beta-cells (2020)
Figure 2

Figure 2. Deletion of Abca12 in β-cells leads to glucose insensitivity.

(A-F) Oral and intraperitoneal glucose tolerance testing in Abca12tm1d mice at 6 (A,B), 8 (C, D) and 12 weeks (E,F) (mean±SEM, n=4-9 mice per group, * p=<0.05, **p<0.01 Students t-test).

(G) Insulin tolerance in 12 week old mice (mean±SEM, n=4-9 mice per group).

(H) Whole blood Hb1Ac levels in 16 week old Abca12tm1d mice (mean±SEM, n=4-9 mice per group, **p<0.01 Students t-test).

(I) Acute phase insulin secretion after intraperitoneal injection of glucose (mean±SEM, n=4-9 animals per group, white/grey/black = Abca12+/+, cre/+ and Abca12tm1d respectively, mice at 8 weeks of age, **p<0.01 Students t-test).

(J) Silencing of ABCA12 in MIN6 cells as assessed by Western blot of ABCA12 immuno-precipitate (top panel) or confocal microscopy in cells transfected with Dy547-siRNAABCA12 (lower panel, scale bar = 10μm).

(K) Glucose stimulated insulin secretion (GSIS) from MIN6 cells after silencing of ABCA12 (mean±SEM, n=4 replicates from assays in quadruplicate, ***p<0.0001, Students t-test).

(L) Cellular insulin content in MIN6 cells after silencing of ABCA12 (mean±SEM, n=4 replicates from assays in quadruplicate).
ABCA12 regulates insulin secretion from beta-cells (2020)
Figure 3

Figure 3. Loss or depletion of ABCA12 results in defects in GSIS independently of changes in cholesterol levels and ABCA1, ABCG1 and LXRβ.

(A-C) (A) ABCA1, (B) ABCG1 and (C) LXRβ expression in islets of 8 week old mice assessed by Western blotting (mean±SEM, n=3-6 mice per genotype, relative to β-actin controls, *p<0.05, **p=<0.01, Students t-test).

(D) Western blot of cell lysates of MIN6 cells after silencing of Abca12, probed with antibodies against ABCA1, ABCG1, SR-B1 and LXRβ.

(E) Total cholesterol (COH) or cholesteryl esters (CE) levels in isolated pancreatic islets of mice at 8 weeks of age with deletion of Abca12 in β-cells (mean±SEM n=9, 5 and 5 mice per genotype respectively).

(F) Ceramides levels in isolated pancreatic islets of mice at 8 weeks of age with deletion of Abca12 in β-cells (mean±SEM n=10, 4 and 5 mice per genotype respectively).

(G) Lipid levels in MIN6 cells in which ABCA12 had been depleted by siRNA treatment (mean±SEM, n=5 (biological replicates assayed in triplicate), FC = free cholesterol, CE = cholesterol ester, Cer = ceramide, SM = sphingomyelin, TG = triacylglycerol, PC = phosphatidylcholine, *p<0.05, **p=<0.01, Students t-test).

(H) Cholesterol efflux to lipid-free apoA-I (30 μg/ml, 2 h) from MIN6 cells transfected with siRNAscr or siRNAABCA12 and activated or not with TO901317 (4 μM)(mean±SEM, n=4, (biological replicates assayed in triplicate), *p=<0.05, Students t-test).

(I) Cholesterol efflux to HDL (30 μg/ml, 2 h) from MIN6 cells transfected with siRNAscr or siRNAABCA12 and activated or not with TO901317 (4 μM); (mean±SEM, n=4 (biological replicates assayed in triplicate)).

(J) The effect of overexpression of ABCA1 on GSIS from MIN6 cells with ABCA12 deficiency (mean±SEM, n=4 (biological replicates assayed in triplicate), *p=<0.05, Students t-test), inset shows a Western blot of cell lysates probed with anti-ABCA1 antibody in which the order of bands corresponds to the order of bars).

(K) The effect of overexpression of ABCG1 on GSIS from MIN6 cells with ABCA12 deficiency (mean±SEM, n=4 (biological replicates assayed in triplicate), *p=<0.05, Students t-test, inset shows a Western blot of cell lysate probed with anti-ABCG1 anitbodies in which the order of bands corresponds to the order of bars).

(L) The effect of overexpression of ABCA1 and ABCG1 on GSIS from MIN6 cells with ABCA12 deficiency (mean±SEM, n=4 (biological replicates assayed in triplicate), *p=<0.05, Students t-test).

(M) The effect of activation of cells with TO901317 (4 μM) on GSIS from MIN6 cells with ABCA12 deficiency (mean±SEM, n=4 (biological replicates assayed in triplicate), *p=<0.05, Students t-test).

(N) The effect of overexpression of LXRβ on GSIS from MIN6 cells with ABCA12 deficiency (mean±SEM, n=4 (biological replicates), *p=<0.05, Students t-test, inset shows a Western blot of cell lysates probed with anti-LXRβ antibody in which the order of bands corresponds to the order of bars).
ABCA12 regulates insulin secretion from beta-cells (2020)
Figure 4

Figure 4 Changes in gene expression and insulin granule fusion in Abca12tm1d mice.

(A) Clustering of gene expression by genotype in RNAseq of islets isolated of cre control and Abca12tm1d mice at 8 weeks of age.

(B) Scatter plot and heat map of differential gene expression between cre control and Abca12tm1d mice at 8 weeks of age. Legend indicates Log2 fold change values.

(C) Circulating glucose levels after administration of intraperitoneal L-arginine in mice at 8 weeks of age, mean±SEM, n =3 mice per genotype, *p=<0.05 of cre relative to tm1d, Students t-test). (D) Representative images of insulin granule fusion events (yellow circles) in mice of indicated genotypes in response to administration of 15mM glucose (scale bar = 10μm). Quantification of the proportion of responding cells and the density of granule fusion events are presented in graphs in the lower panel (mean±SEM, 8-10 islets/mouse, >4 mice/genotype, **p=<0.01, ***p=<0.001 of cre relative to tm1d, Students t-test).

(E) Representative images of insulin granule fusion events (yellow circles) in mice of indicated genotypes in response to administration of 20mM KCl (scale bar = 10μm). Quantification of the proportion of responding cells and the density of granule fusion events are presented in graphs in the right panel (mean±SEM, 8-10 islets/mouse, >4 mice/genotype, **p=<0.01 of cre relative to tm1d, Students t-test).

(F) Assessment of calcium flux measured by Fluo4 in response to either Glucose or Potassium in isolated islets from 11 week old animals. Fluorescence responses were corrected for basal fill (F/F0). (mean±SEM, each data point represents the average of 10 cells/coverslip for 13-16 coverslips for each of 4 wild type and 5 Abca12tm1d mice)

(G) Expression of GLUT2 in isolated mouse islets at 8 weeks of age. The upper panel depicts a representative Western blot and the lower graph the quantitation of protein levels from 3 mice of each genotype, normalised to β-actin (mean±SEM).

(H) Insulin content of islets of Abca12tm1d mice (mean±SEM, n=3 mice of each genotype, normalised to total protein content).
ABCA12 regulates insulin secretion from beta-cells (2020)
Figure 5

Figure 5. Loss of β-cell ABCA12 leads to cholesterol modulated changes in insulin granule morphology.

(A-C) Transmission electron microscopy of β-cells from Abca12tm1d and control mice at 8 weeks of age. Panels A'-C' depict higher resolution images from the boxed regions in A-C (scale bar = 1μm). (D) Quantitation of the area of 3000 granules from each genotype (mean±SEM, n=4, 3 and 3 animals respectively, *p=<0.05 of cre relative to tm1d, Students t-test).

(E) Relative frequency distribution of granule areas from (D).

(F) Assessment of total cholesterol (COH) by mass spectroscopy in mice fed normal chow or a high cholesterol diet (HCD)(mean±SEM, n=5 and 4 animals respectively, **p=<0.01, Students t-test).

(G, H) Quantification of change in mean granule area in Abca12tm1d on chow diet and Abca12tm1d on high cholesterol diet islets assessed by transmission electron microscopy (n=3000 granules/genotype, mean±SEM, n=4, 3, 3 and 4 animals respectively, *p=<0.05, Students t-test) as an average and as a relative frequency distribution.

(I) Correction in abnormal granule shape following high cholesterol feeding (bar = 1μm), with I' showing magnification of the boxed region indicated.

(J) Glucose tolerance test results following intraperitoneal glucose challenge in Abca12tm1d and cre control mice fed normal chow or HCD (mean±SEM, n=3 mice per genotype, *p=<0.05, for tm1d versus tm1d+HCD, Students t-test).

(K) Serum insulin in Abca12tm1d +/- HCD mice after i.p glucose challenge (mean±SEM, n=3 mice/genotype, **p=<0.01, Students t-test).
ABCA12 regulates insulin secretion from beta-cells (2020)
Figure 6

Figure 6 Loss of Abca12 results in altered lipid raft levels and changes in F-actin and CDC42 activity.

(A) Detection of lipid rafts in 8 week old islets with recombinant cholera toxin subunit B (CT-B) conjugated to Alexa Fluor 488 (green). Islets are co-stained with DAPI (blue) (scale bar = 50μm.).

(B) FACS profiling of dispersed islets from 12 week old mice stained with insulin and CT-B.

(C) Confocal images of rafts (using CTB-Alexa Fluor 647) in MIN6 cells transfected with Fluorescein-488-labelled siRNAScr or Dy547-labelled siRNAABCA12 (scale bar=10μm).

(D) Quantitation by confocal microscopy of the effect of ABCA12-deficincy on CTB binding to MIN6 cells (mean±SEM, *p=<0.05, Students t-test, n=4 biological replicates, 50-100 cells for each).

(E) Quantitation by flow cytometry of the effect of ABCA12-deficiency on CTB binding to MIN6 cells (mean±SEM, n=3 biological replicates, *p=<0.05, Students t-test).

(F) The effect 10 mM MβCD on GSIS in MIN6 cells depleted or not for ABCA12 (incubation for 5 or 10 minutes as indicated, mean±SEM, n=4 (biological replicates), *p=<0.05, Students t-test).

(G) Western blot of the abundance of CDC42 in ABCA12 deficient MIN6 cells.

(H) The effect of ABCA12 deficiency on activation of CDC42 by bradykinin in MIN6 cells (BDK, 100 ng/ml, 4 min; *p=<0.05, Students t-test, significance versus ABCA12-deficient BDK activated cells is indicated, n=4 biological replicates, mean±SEM).

(I,J) (I) Confocal images of F-actin in ABCA12-deficient MIN6 cells (scale bar = 20μm) and (J) quantification of abundance showing the effect of ABCA12-deficiency (mean±SEM, *p=<0.05, Students t-test, n=4 biological replicates, 50-100 cells for each).

(K) F-actin levels assessed by FACS sorting of labelled MIN6 cells transfected with siRNAABCA12 (mean±SEM, n=3 biological replicates, *p=<0.05, Students t-test).

(L,M) (L) Representative image of F-actin using LifeAct staining of purified islets isolated from Abca12tm1d versus control mice (scale bar = 10μm) and (M) quantitation of fluorescent signals from these samples (n=3 biological replicates, mean±SEM, ***p=<0.001, ****p=<0.0001 Students t-test).

(N) Colocalization between ABCA12 (red) and CDC42 (green) in MIN6 cells (scale bar = 10μm).

O) Effects of overexpression of a constitutively active form of CDC42 on GSIS from MIN6 cells with ABCA12-deficiency (mean±SEM, n=4 biological replicates, *p=<0.05, Students t-test).

(P) The effect of overexpression of consitutively active CDC42 on ABCA1 abundance in MIN6 cells with ABCA12-deficiency. Treatments are defined in the table below.

(Q) Effects of Jasplakinolide on F-actin levels (green) in siRNA treated cells (scale bar=10μm).

(R) Effects of Abca12 knockdown and Jasplakinolide treatment on MIN6 cell in low and high glucose (mean±SEM, n=4 biological replicates, *p=<0.05, **p=<0.01, significance relative to untreated cells, Students t-test)
ABCA12 regulates insulin secretion from beta-cells (2020)
Figure 7

Figure 7 Aging of Abca12tm1d mice leads to the development of lipid imbalance and progressive inflammatory disease.

(A) Mass spectroscopy analysis of levels of cholesterol and cholesteryl esters in purified islets from Abca12tm1d mice versus control animals at 16 weeks of age (mean±SEM, n=10, 4 and 5 mice per genotype respectively; COH=cholesterol, CE=cholesteryl ester).

(B) Mass spectroscopy analysis of lipids families in purified islets from Abca12tm1d mice versus control animals at 16 weeks of age (mean±SEM, n=10, 4 and 5 mice per genotype respectively, **p=<0.01 Students t-test); CE=cholesteryl ester, Cer=ceramide, DHC (Hex2Cer)=dihexosylceramide, MHC (HexCer)=monohexosylceramide, SM=sphingomyelin, GM3=GM3 ganglioside, dhCer=dihydroceramide, DG=diacylglyerol, TG=triacylglycerol).

(C) Mass spectroscopy analysis of triglyceride species in purified islets from Abca12tm1d mice versus control animals at 16 weeks of age (mean±SEM, n=10, 4 and 5 mice per genotype respectively, *p=<0.05, **p=<0.01, Students t-test)

(D) Immunohistochemical staining of levels IL-1β expression in sections of pancreas from Abca12tm1d mice versus control animals at 24 weeks of age (bar = 25μm, islets outlined).

(E) Quantification of islet specific IL1β staining from sections of Abca12tm1d, Cre and wild type mice (mean±SEM, n=3, 3 and 4 mice of each genotype respectively; *p=<0.05, Students t-test).

(F-I) Analysis of Abca12tm1d pancreata from mice at 24 weeks of age compared to control mice assessing β-cell mass (F), cleaved caspase 3 (G), glucagon (H) and F480+ macrophage populations (I)(mean±SEM, n=3-9 mice per genotype, **p=<0.01, ***p=<0.001, Students t-test). (J) Fasting blood glucose levels coincident with the emergence of inflammatory phenotypes (mean±SEM, n=3, 4 and 5 mice per genotype respectively, *p=<0.05, Students t-test).
Neutrophils induce paracrine telomere dysfunction and senescence in ROS-dependent manner. (2021)
Figure 1

Fig 1 Neutrophils induce paracrine senescence

a) Schematic depicting experimental design.;

b) effect of neutrophils and recombinant catalase on population doublings (data are from 3 independent cultures are shown). Blue arrow indicates time point in which neutrophils were added to culture for consecutive 3 days;

c) % ∆ Population Doublings (PD) following neutrophil co-culture;

d) representative images of Ki67 and p16Ink4a immunofluorescence and SA-β-Gal staining;

e) % of Ki67 positive cells (28 days after co-culture);

f) % of p16INK4A positive cells (28days after co-culture);

g) % of SA-β-Gal positive cells (28 days after co-culture);

h) Western blotting for p21 and quantification;

i) MitoSOX fluorescence;

j) Heat map depicting expression of 48 human cytokines in conditioned media at 8 and 28 days following co-culture.

Data information: Data are mean±S.E.M. of 3 independent experiments. Statistical analysis was performed using one‐way ANOVA (Holm-Sidak method) for multiple comparisons and two‐tailed t‐test for single comparisons. **P < 0.01; *P < 0.04.
Neutrophils induce paracrine telomere dysfunction and senescence in ROS-dependent manner. (2021)
Figure 2

Fig 2 Neutrophils induce paracrine senescence via telomere dysfunction

a) Histograms representing distribution of individual telomere FISH intensities at day 4 and 16 following co-culture with neutrophils. Dotted blue lines represent median telomere FISH fluorescence. Data are from n=3 independent experiments;

b) Representative micrographs of telomere FISH in metaphases;

c) Mean telomere FISH intensity at 4 and 16 days following co-culture with neutrophils represented as mean±s.e.m of 3 independent experiments;

d) Representative Immuno-FISH micrographs (using telomere‐specific (CCCTAA) peptide nucleic acid probe and anti-γH2A.X antibody). Arrows indicate co-localization between telomeres and γH2A.X;

e) Mean number and % of Telomere-associated DDR foci (TAF). Data are mean±S.E.M. of 3 independent experiments;

f) Population doublings of hTERT expressing MRC5 fibroblasts or controls following co-culture with primed neutrophils (data are representative of 6 independent experiments);

g) histograms representing distribution of individual telomere FISH intensities in MRC5 fibroblasts expressing hTERT 16 days following neutrophil co-culture. Dotted blue lines represent median telomere FISH fluorescence.;

h) Representative Immuno-FISH micrographs (using telomere‐specific (CCCTAA) peptide nucleic acid probe and anti-53BP1 antibody) 20 days following co-culture;

i) quantification of mean TAF and % TAF in MRC5 fibroblasts 8 and 20 days following neutrophil co-culture. Data are mean±S.E.M. of 3 independent experiments;

J-L) mRNA expression of p21 (j), IL-6 (k) and IL-8 (l) 20 days after neutrophil co-culture; Data are mean±S.E.M. of 2-3 independent experiments.

m) western blot and quantification of p21 and LaminB1 20 days after neutrophil co-culture. Data are mean±S.E.M. of 2 independent experiments.

Data information: Statistical analysis was performed using one‐way ANOVA (Holm-Sidak method) for multiple comparisons and Mann-Whitney test and two‐tailed t‐test for single comparisons. **P < 0.01; *P < 0.04.
Neutrophils induce paracrine telomere dysfunction and senescence in ROS-dependent manner. (2021)
Figure 3

Fig 3 Neutrophils induce telomere dysfunction and senescence in human Precision-cut liver slices (PCLS)

a) Schematic depicting experimental design.;

b) Representative micrographs of neutrophil marker CD66B;

c) Quantification of neutrophil counts per field;

d) Lactate dehydrogenase (LD) activity as a function of time in bioreactor;

e) representative Immuno-FISH micrographs (using telomere‐specific (CCCTAA) peptide nucleic acid probe and anti-γH2A.X antibody). Arrow indicates co-localization between telomeres and γH2A.X;

f) mean number of TAF in hepatocytes;

g) % of TAF positive hepatocytes;

h) number of p21 positive hepatocytes per field;

i) number of p16Ink4a positive hepatocytes per field.

Data information: Data are mean ± S.E.M from liver biopsies obtained from 7 male patients aged between 49 and 72 years. Neutrophils were isolated from healthy individuals aged between 21-30 years (with purity above 90%). Statistical analysis was performed using one‐way ANOVA (Holm-Sidak method) for multiple comparisons and two‐tailed t‐test for single comparisons. **P < 0.01; *P < 0.04.
Neutrophils induce paracrine telomere dysfunction and senescence in ROS-dependent manner. (2021)
Figure 4

Fig 4 Neutrophils induce telomere dysfunction in a ROS-dependent manner in Precision-cut liver slices (PCLS).

a) Schematic depicting experimental design;

b) mRNA expression of hCAT in bone marrow derived neutrophils from wild-type and MCAT mice;

c) catalase activity in bone marrow derived neutrophils from wild-type and MCAT mice;

d) Dihydrorhodamine 123 fluorescence was assessed by flow cytometry in neutrophils from wild-type and MCAT mice with or without stimulation with PMA;

e) Representative micrographs of neutrophil marker Ly6G and senescent-associated marker p21 (96h);

f) number of Ly6G positive cells per field (96h);

g) % of TAF positive hepatocytes (96h);

h) mean number of TAF in hepatocytes (96h);

i) total number of γH2A.X foci in hepatocytes (96h);

j) Lactate dehydrogenase (LD) activity (96h);

k) p21 positive cells per field (96h).

Data information: Data are mean±s.e.m. of 3-5 independent PCLS. Statistical analysis was performed using one‐way ANOVA (Holm-Sidak method) for multiple comparisons and two‐tailed t‐test for single comparisons. **P < 0.01; *P < 0.04.
S-acylated Golga7b stabilises DHHC5 at the plasma membrane to regulate cell adhesion (2019)
Figure 1

Figure 1: A palmitoylation-dependent interaction between DHHC5 and Golga7b.

(A) Immunoblots of acyl-biotin exchange purifications from Hela cells transiently transfected with WT Golga7b or a palmitoylation-deficient mutant form of the protein with cysteines replaced with alanine residues. The hydroxylamine sensitivity of the Golga7b signal in the + HA condition of the WT pull-down and not in either the - HA condition or the + HA condition of the mutant shows that Golga7b is a palmitoylated protein.

(B) Immunoblots of acyl-biotin exchange purifications from Hela cells treated with either DHHC5 siRNA or control non-targeting siRNA.

(C) Immunoblots showing rescue of Golga7b palmitoylation in DHHC5 depleted cells after transfection of WT DHHC5 but not by the DHHC5 catalytic mutant.

(D) A significant reduction in the Golga7b signal is observed in the + HA condition of the pull-down when DHHC5 is depleted with siRNA. The graph displays mean +/- s.e.m. N=4, *=p<0.05, paired t-test.

(E) Immunoblots of WT and non-palmitoylatable mutant Golga7b from immunoprecipitations of WT DHHC5 and a pair of DHHC5 mutants (DHHS5 = catalytically inactive mutant where catalytic cysteine has been mutated to serine, C-terminal mutant = mutant where the 3 C-terminal palmitoylation sites of DHHC5 have been mutated to alanine residues.). WT and DHHS5 immunoprecipitates both WT and mutant Golga7b but the C-terminal mutant is unable to immunoprecipitate either form of Golga7b showing that the palmitoylation of the C-terminus of DHHC5 is essential for the stability of this interaction.
S-acylated Golga7b stabilises DHHC5 at the plasma membrane to regulate cell adhesion (2019)
Figure 2

Figure 2: Regulation of DHHC5 localisation by palmitoylation of Golga7b and the C-terminus of DHHC5.

Tagged constructs with palmitoylation site mutations in DHHC5 and Golga7b were expressed in in HeLa cells depleted of endogenous DHHC5.

( A) Confocal images of HeLa cells co-expressing WT Golga7b (1st column) and DHHC5 (2nd column), with a merged image (3rd column).

(B) Confocal images of HeLa cells co-expressing palmitoylation deficient mutant Golga7b (1st column) and DHHC5 (2nd column), with a merged image (3rd column).

(C) Confocal images of HeLa cells co-expressing WT Golga7b (1st column) and the catalytic mutant DHHS5 (2nd column), with a merged image (3rd column).

(D) Confocal images of HeLa cells co-expressing palmitoylation deficient mutant Golga7b (1st column) and DHHS5 (2nd column), with a merged image (3rd column).

(E) Confocal images of HeLa cells co-expressing WT Golga7b (1st column) and DHHC5 C-terminal palmitoylation deficient mutant (2nd column), with a merged image (3rd column).

(F) Confocal images of HeLa cells co-expressing palmitoylation deficient mutant Golga7b (1st column) and DHHC5 C-terminal palmitoylation deficient mutant (2nd column), with a merged image (3rd column).

(G) Quantification of the plasma membrane signal of DHHC5 in each of the images (A-F), the graph displays mean +/- s.e.m. ****=p<0.001, n.s. = not significant, unpaired t-test. N=35, DHHC5 + WT Golga7b. N=41, DHHC5 + mutant Golga7b. N=35, DHHS5 + WT Golga7b. N=31, DHHS5 + Golga7b mutant. N=29, C-terminal mutant + WT Golga7b. N=30, C-terminal mutant + mutant Golga7b. Co expression of palmitoylation-deficient mutant Golga7b significantly reduces DHHC5 as well as DHHCS5 signal at the plasma membrane. The majority of the DHHC5 C-terminal palmitoylation-deficient mutant is localised to the plasma membrane in a Golga7b independent manner. All N numbers refer to the number of cells imaged and quantified, all experiments repeated 4 times.

Data information: All images show ectopic protein expression only. All scale bars 10µm.
S-acylated Golga7b stabilises DHHC5 at the plasma membrane to regulate cell adhesion (2019)
Figure 3

Figure 3: Palmitoylated Golga7b stabilises endogenous DHHC5 at the plasma membrane.

(A) Confocal images of endogenous DHHC5 in HeLa cells expressing FLAG-tagged WT Golga7b.

(B) Confocal images of endogenous DHHC5 in HeLa cells expressing FLAG-tagged mutant Golga7b.

(C) Confocal images of endogenous Golga7b and DHHC5 in HeLa cells treated with negative control non-targeting siRNA.

(D) Confocal images of endogenous Golga7b and DHHC5 in HeLa cell treated with Golga7b siRNA.

(E) Quantification of plasma membrane signal of endogenous DHHC5 when co-expressed with WT or mutant Golga7b or without any transfected Golga7b. ****=P<0.001, t-test, endogenous + WT Golga7b n=37, endogenous + mutant Golga7b n=23, endogenous n=42. Expression of the palmitoylation deficient mutant Golga7b causes endogenous DHHC5 to be internalised in the cell, while WT Golga7b stabilises DHHC5 at the plasma membrane.

(F) Quantification of the plasma membrane signal of DHHC5 in (C and D), ****=p<0.001 t-test, control siRNA n=23, Golga7b siRNA n=23.

Data information: All N numbers refer to the number of cells imaged and quantified, all experiments repeated 4 times. Error bars represent s.e.m. All scale bars 10µm.