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A structure-based mechanism for Arf1-dependent recruitment of coatomer to membranes.

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 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 PtdIns4,5P(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.

Pubmed ID: 22304919

Authors

  • Yu X
  • Breitman M
  • Goldberg J

Journal

Cell

Publication Data

February 3, 2012

Associated Grants

  • Agency: NIBIB NIH HHS, Id: P30 EB009998
  • Agency: Howard Hughes Medical Institute, Id:
  • Agency: Howard Hughes Medical Institute, Id:

Mesh Terms

  • ADP-Ribosylation Factor 1
  • Amino Acid Sequence
  • Animals
  • COP-Coated Vesicles
  • Golgi Apparatus
  • Guanosine Triphosphate
  • Intracellular Membranes
  • Models, Molecular
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Sequence Alignment