A Novel GTPase-activating Protein for ARF6 Directly Interacts with Clathrin and Regulates Clathrin-dependent Endocytosis

• DOI: 10.1091/mbc.e04-08-0683
• Publication Date: 2005-01-20T01:33:30Z
• Authors: Kenji Tanabe; Tetsuo Torii; Waka Natsume; Sten Braesch-Ande...; Toshio Watanabe; Masanobu Satake
• Keywords: ADP ribosylation factor; Transferrin receptor; Internalization

ADP-ribosylation factor 6 (Arf6) is a small-GTPase that regulates the membrane trafficking between plasma and endosome. It also involved in reorganization of actin cytoskeleton. GTPase-activating protein (GAP) critical regulator Arf function as it inactivates Arf. Here, we identified novel species GAP denoted SMAP1 preferentially acts on Arf6. Although overexpression did not alter subcellular distribution cytoskeleton, block endocytosis transferrin receptors. Knock down endogenous abolished internalization, which confirms needed for this endocytic process. had no effect clathrin-independent endocytosis, however. Intriguingly, binds directly to clathrin heavy chain via its clathrin-box mutation studies revealed domain both contribute role plays clathrin-dependent endocytosis. These observations suggest may be an Arf6GAP specifically one multiple functions Arf6, namely, does so by binding clathrin.