Author: ["Ming Bai","Helge Gad","Gabriele Turacchio","Emanuele Cocucci","Jia-Shu Yang","Jian Li","Galina V. Beznoussenko","Zhongzhen Nie","Ruibai Luo","Lianwu Fu","James F. Collawn","Tomas Kirchhausen","Alberto Luini","Victor W. Hsu"]
CITE.CC academic search helps you expand the influence of your papers.
Abstract
COPI (coat protein I) and the clathrin–AP-2 (adaptor protein 2) complex are well-characterized coat proteins, but a component that is common to these two coats has not been identified. The GTPase-activating protein (GAP) for ADP-ribosylation factor 1 (ARF1), ARFGAP1, is a known component of the COPI complex. Here, we show that distinct regions of ARFGAP1 interact with AP-2 and coatomer (components of the COPI complex). Selectively disrupting the interaction of ARFGAP1 with either of these two coat proteins leads to selective inhibition in the corresponding transport pathway. The role of ARFGAP1 in AP-2-regulated endocytosis has mechanistic parallels with its roles in COPI transport, as both its GAP activity and coat function contribute to promoting AP-2 transport. ARFGAP1 regulates COPI coat formation and participates in COPI-dependent trafficking. ARFGAP1 is now shown to interact with the clathrin adaptor complex AP-2 through a region distinct from its COP1-interacting domain, and to regulate transport of AP-2 cargo proteins.Cite this article
Bai, M., Gad, H., Turacchio, G. et al. ARFGAP1 promotes AP-2-dependent endocytosis. Nat Cell Biol 13, 559–567 (2011). https://doi.org/10.1038/ncb2221 