A Structure-based mechanism for Arf1-dependent recruitment of coatomer to membranes Journal Article


Authors: Yu, X.; Breitman, M.; Goldberg, J.
Article Title: A Structure-based mechanism for Arf1-dependent recruitment of coatomer to membranes
Abstract: 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. © 2012 Elsevier Inc.
Keywords: chemical analysis; protein interaction; binding site; protein structure; guanosine triphosphate; membrane binding; endosome; clathrin; coatomer protein; adenosine diphosphate ribosylation factor 1; coat protein; trans golgi network
Journal Title: Cell
Volume: 148
Issue: 3
ISSN: 0092-8674
Publisher: Cell Press  
Date Published: 2012-02-03
Start Page: 530
End Page: 542
Language: English
DOI: 10.1016/j.cell.2012.01.015
PROVIDER: scopus
PMCID: PMC3285272
PUBMED: 22304919
DOI/URL:
Notes: --- - "Export Date: 1 March 2012" - "CODEN: CELLB" - "Source: Scopus"
Altmetric
Citation Impact
BMJ Impact Analytics
MSK Authors
  1. Xinchao Yu
    1 Yu