Arf6 regulates AP-1B-dependent sorting in polarized epithelial cells

Elina Shteyn, Lucy Pigati, Heike Fölsch*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)873-887
Number of pages15
JournalJournal of Cell Biology
Issue number6
StatePublished - Sep 19 2011

ASJC Scopus subject areas

  • Cell Biology


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