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. 2016 Nov 15;27(23):3771–3779. doi: 10.1091/mbc.E15-11-0757

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© 2016 Skorobogata, Meng, 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 3: — DHC-1 and RAB-7 differentially regulate LET-23 EGFR trafficking. (A–H) Representative confocal images of LET-23::GFP localization in the P6.p daughter cells—P6.pa and P6.pp—of zhIs038 transgene-carrying animals. The receptor is localized to both basolateral and apical membranes of wild-type animals (A) but is restricted to the apical membrane in lin-2(e1309) animals (B). rab-7(ok511) and dhc-1(vh22) mutants accumulate LET-23::GFP in the punctate structures within the vulval cells (C, D) and adjacent to the plasma membrane (E, F), respectively, in both wild-type (C, E) and lin-2(e1309) backgrounds. (G) dhc-1(or195) mutants also accumulate LET-23::GFP foci at 25°C. (H) dhc-1(RNAi) does not significantly change the dhc-1(vh22); lin-2(e1309) phenotype. (I, J) Box-and-whiskers plots of the number of LET-23::GFP foci in the P6.p descendants for the indicated genotypes. The number of animals scored is indicated above. (I) Number of cytoplasmic (pink), juxtamembrane (green), and combined total (yellow) LET-23::GFP foci. For statistical analysis, the average number of foci in the rab-7(ok511), dhc-1(vh22), and dhc-1(or195) mutants was compared with wild type. The dhc-1(vh22); rab-7(ok511) double was compared with the dhc-1(vh22) mutant and was not significantly different from rab-7(ok511). (J) Total number of LET-23::GFP foci. All double mutants were compared with lin-2(e1309). dhc-1(vh22+RNAi); lin-2(-) was not statistically different from dhc-1(vh22); lin-2(-). A two-tailed t test was used to calculate statistical significance (*p < 0.05, **p < 0.01, ****p < 0.0001). Basal and apical membranes are facing in the same direction in all of the images and are indicated in A. Bar, 5 μm.