A Structure-Based Mechanism for Arf1-Dependent Recruitment of Coatomer to Membranes

SummaryBudding 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 γζ-COP subcomplex of coatomer. Structure-guided biochemical analysis reveals that a second Arf1-GTP molecule binds to βδ-COP at a site common to the γ- and β-COP subunits. The Arf1-binding sites on coatomer are spatially related to PtdIns4,5P2-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.

Graphical AbstractFigure optionsDownload high-quality image (302 K)Download as PowerPoint slideHighlights
► Structural analysis shows how Arf1 binds to the coatomer subcomplex γζ-COP
► Biochemical analysis reveals that an Arf1 molecule also binds to βδ-COP
► Results support a model for bivalent interaction of coatomer with Golgi membranes