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Published 28 March 2005. doi:10.1083/jcb.200410142
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 7, 1053-1063
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Article

 ArfGAP1 dynamics and its role in COPI coat assembly on Golgi membranes of living cells

Wei Liu1, Rainer Duden3, Robert D. Phair2, and Jennifer Lippincott-Schwartz1

1 Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892
2 Bioinformatics Services, Rockville, MD 20851
3 School of Biological Sciences, Royal Holloway, University of London, UK

Correspondence to Jennifer Lippincott-Schwartz: jlippin{at}helix.nih.gov

Secretory protein trafficking relies on the COPI coat, which by assembling into a lattice on Golgi membranes concentrates cargo at specific sites and deforms the membranes at these sites into coated buds and carriers. The GTPase-activating protein (GAP) responsible for catalyzing Arf1 GTP hydrolysis is an important part of this system, but the mechanism whereby ArfGAP is recruited to the coat, its stability within the coat, and its role in maintenance of the coat are unclear. Here, we use FRAP to monitor the membrane turnover of GFP-tagged versions of ArfGAP1, Arf1, and coatomer in living cells. ArfGAP1 underwent fast cytosol/Golgi exchange with ~40% of the exchange dependent on engagement of ArfGAP1 with coatomer and Arf1, and affected by secretory cargo load. Permanent activation of Arf1 resulted in ArfGAP1 being trapped on the Golgi in a coatomer-dependent manner. These data suggest that ArfGAP1, coatomer and Arf1 play interdependent roles in the assembly–disassembly cycle of the COPI coat in vivo.

Abbreviations used in this paper: BFA, brefeldin A; FLIP, fluorescence loss in photobleaching; GAP, GTPase-activating protein.


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