Affiliation:
1. Department of Cell Biology, Faculty of Science Charles University Viničná 7 Prague Czech Republic
Abstract
AbstractThe pentameric WASH complex facilitates endosomal protein sorting by activating Arp2/3, which in turn leads to the formation of F‐actin patches specifically on the endosomal surface. It is generally accepted that WASH complex attaches to the endosomal membrane via the interaction of its subunit FAM21 with the retromer subunit VPS35. However, we observe the WASH complex and F‐actin present on endosomes even in the absence of VPS35. We show that the WASH complex binds to the endosomal surface in both a retromer‐dependent and a retromer‐independent manner. The retromer‐independent membrane anchor is directly mediated by the subunit SWIP. Furthermore, SWIP can interact with a number of phosphoinositide species. Of those, our data suggest that the interaction with phosphatidylinositol‐3,5‐bisphosphate (PI(3,5)P2) is crucial to the endosomal binding of SWIP. Overall, this study reveals a new role of the WASH complex subunit SWIP and highlights the WASH complex as an independent, self‐sufficient trafficking regulator.
Funder
European Regional Development Fund
Grantová Agentura, Univerzita Karlova
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology
Cited by
2 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献