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Published 18 January 2005. doi:10.1083/jcb.200404008
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 2, 281-290
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Article

 ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation

Stella Y. Lee1, Jia-Shu Yang1, Wanjin Hong2, Richard T. Premont3, and Victor W. Hsu1

1 Division of Rheumatology, Immunology, and Allergy, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, MA 02115
2 Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609
3 Department of Medicine, Division of Gastroenterology, Duke University Medical Center, Durham, NC 27710

Correspondence to Victor W. Hsu: vhsu{at}rics.bwh.harvard.edu

Examining how key components of coat protein I (COPI) transport participate in cargo sorting, we find that, instead of ADP ribosylation factor 1 (ARF1), its GTPase-activating protein (GAP) plays a direct role in promoting the binding of cargo proteins by coatomer (the core COPI complex). Activated ARF1 binds selectively to SNARE cargo proteins, with this binding likely to represent at least a mechanism by which activated ARF1 is stabilized on Golgi membrane to propagate its effector functions. We also find that the GAP catalytic activity plays a critical role in the formation of COPI vesicles from Golgi membrane, in contrast to the prevailing view that this activity antagonizes vesicle formation. Together, these findings indicate that GAP plays a central role in coupling cargo sorting and vesicle formation, with implications for simplifying models to describe how these two processes are coupled during COPI transport.

Abbreviations used in this paper: ARF, ADP ribosylation factor; COPI, coat protein I; GAP, GTPase-activating protein.


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