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. 2017 Nov 1;28(22):3095–3111. doi: 10.1091/mbc.E17-06-0421

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© 2017 Copeland, Han, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 1: — CAV1 P158 is targeted to the ER and lipid droplets as the result of the introduction of a functional ER retention signal by the frameshift mutation. (A–E) Immunofluorescence staining of WT CAV1, CAV1-P158, CAV1-P158-AAYK, CAV1-P158-ΔKKYK, and CAV1-KKYK (green) expressed in Cav1^–/– MEFs. Cells were colabeled with the ER marker calreticulin (CalR, red) and the lipid droplet marker ADRP (cyan). The dashed box indicates the region shown in the zooms. Scale bars = 10 μm. (F, G) Quantification of the extent of colocalization between CAV1 constructs with CalR or ADRP, respectively, calculated by Pearson’s correlation. The data were analyzed with a nonparametric Kluskal–Wallis test and post hoc Dunn’s multiple comparisons test to calculate p values. Data are averaged over three independent experiments for the following numbers of regions of interest (ROIs): Calreticulin/WT CAV1, n = 33; calreticulin/CAV1-P158, n = 30; calreticulin/CAV1-P158-AAYK, n = 52; calreticulin/CAV1-P158-ΔKKYK, n = 43; calreticulin/CAV1-KKYK, n = 40; ADRP/WT CAV1, n = 85; ADRP/CAV1-P158, n = 73; ADRP/CAV1-P158-AAYK, n = 104; ADRP/CAV1-P158-ΔKKYK, n = 107; and ADRP/CAV1-KKYK, n = 114. Asterisks (*) and hashtags (#) indicate statistically significant differences compared with wild-type CAV1 and CAV1-P158, respectively. ^***/###, p < 0.001.