期刊
CELL
卷 148, 期 3, 页码 530-542出版社
CELL PRESS
DOI: 10.1016/j.cell.2012.01.015
关键词
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资金
- Howard Hughes Medical Institute Funding Source: Medline
- NIBIB NIH HHS [P30 EB009998] Funding Source: Medline
Budding of COPI-coated vesicles from Golgi membranes requires an Arf family G protein and the coatomer complex recruited from cytosol. Arf is also required with coatomer-related clathrin adaptor complexes to bud vesicles from the trans-Golgi network and endosomal compartments. To understand the structural basis for Arf-dependent recruitment of a vesicular coat to the membrane, we determined the structure of Arf1 bound to the gamma zeta-COP subcomplex of coatomer. Structure-guided biochemical analysis reveals that a second Arf1-GTP molecule binds to beta delta-COP at a site common to the gamma-and beta-COP subunits. The Arf1-binding sites on coatomer are spatially related to PtdIns4,5P(2)-binding sites on the endocytic AP2 complex, providing evidence that the orientation of membrane binding is general for this class of vesicular coat proteins. A bivalent GTP-dependent binding mode has implications for the dynamics of coatomer interaction with the Golgi and for the selection of cargo molecules.
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