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- W2098678016 abstract "The epithelial cell–specific clathrin adaptor complex AP-1B facilitates the sorting of various transmembrane proteins from recycling endosomes (REs) to the basolateral plasma membrane. Despite AP-1B’s clear importance in polarized epithelial cells, we still do not fully understand how AP-1B orchestrates basolateral targeting. Here we identify the ADP-ribosylation factor 6 (Arf6) as an important regulator of AP-1B. We show that activated Arf6 pulled down AP-1B in vitro. Furthermore, interfering with Arf6 function through overexpression of dominant-active Arf6Q67L or dominant-negative Arf6D125N, as well as depletion of Arf6 with short hairpin RNA (shRNA), led to apical missorting of AP-1B–dependent cargos. In agreement with these data, we found that Arf6 colocalized with AP-1B and transferrin receptor (TfnR) in REs. In addition, we observed specific recruitment of AP-1B into Arf6-induced membrane ruffles in nonpolarized cells. We conclude that activated Arf6 directs membrane recruitment of AP-1B, thus regulating AP-1B’s functions in polarized epithelial cells." @default.
- W2098678016 created "2016-06-24" @default.
- W2098678016 creator A5025885436 @default.
- W2098678016 creator A5043677886 @default.
- W2098678016 creator A5046080382 @default.
- W2098678016 date "2011-09-12" @default.
- W2098678016 modified "2023-09-26" @default.
- W2098678016 title "Arf6 regulates AP-1B–dependent sorting in polarized epithelial cells" @default.
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- W2098678016 doi "https://doi.org/10.1083/jcb.201106010" @default.
- W2098678016 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3207291" @default.
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