ACBD5 phospho-sites alter peroxisome–ER associations.(A) Representative electron micrographs of peroxisome–ER contacts in ACBD5 KO HeLa cells transfected with Myc-ACBD5 WT, S259A, S261A, S259A/S261A/S263A, S269E, or control vector (Myc). (B) Quantitative analysis of the mean population of peroxisomes associated with the ER. (C) Assessment of the mean peroxisome membrane surface in direct contact with the ER. Data were analyzed by one-way ANOVA with Dunnett’s multiple comparison test; *, P < 0.05; **, P < 0.01; ***, P < 0.001. Results of four grids per condition. (D) Immunoblots of cell lysates from ACBD5 KO HeLa cells expressing the indicated Myc-ACBD5 constructs. αTubulin/Myc (unspecific band) served as loading control. Bars: 200 nm. Source data are available for this figure: SourceData F4.
Figure 4.

ACBD5 phospho-sites alter peroxisome–ER associations. (A) Representative electron micrographs of peroxisome–ER contacts in ACBD5 KO HeLa cells transfected with Myc-ACBD5 WT, S259A, S261A, S259A/S261A/S263A, S269E, or control vector (Myc). (B) Quantitative analysis of the mean population of peroxisomes associated with the ER. (C) Assessment of the mean peroxisome membrane surface in direct contact with the ER. Data were analyzed by one-way ANOVA with Dunnett’s multiple comparison test; *, P < 0.05; **, P < 0.01; ***, P < 0.001. Results of four grids per condition. (D) Immunoblots of cell lysates from ACBD5 KO HeLa cells expressing the indicated Myc-ACBD5 constructs. αTubulin/Myc (unspecific band) served as loading control. Bars: 200 nm. Source data are available for this figure: SourceData F4.

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