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MBC in Press, published online ahead of print November 14, 2007
Mol. Biol. Cell 10.1091/mbc.E07-04-0394

A more recent version of this article appeared on February 1, 2008
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Submitted on May 1, 2007
Revised on October 31, 2007
Accepted on November 6, 2007

Distinct Functions for Arf Nucleotide Exchange Factors at the Golgi Complex: GBF1 and BIGs Are Required for Assembly and Maintenance of the Golgi Stack and TGN, Respectively

Florin Manolea,* Alejandro Claude,{dagger} Justin Chun,* Javier Rosas,{dagger} and Paul Melançon*

*Department of Cell Biology, University of Alberta, Edmonton, AB, T6G 2H7 Canada; {dagger}Instituto de Bioquímica, Universidad Austral de Chile, Valdivia, Chile

Monitoring Editor: Benjamin Glick

We examined the relative function of the two classes of guanine nucleotide exchange factors (GEFs) for ADP-ribosylation factors that regulate recruitment of coat proteins on the Golgi complex. Complementary overexpression and RNA-based knockdown approaches established that GBF1 regulates COPI recruitment on cis-Golgi compartments, while BIGs appear specialized for adaptor proteins on the trans-Golgi. Knockdown of GBF1 and/or COPI did not prevent export of VSVGtsO45 from the ER, but caused its accumulation into peripheral vesiculo-tubular clusters. In contrast, knockdown of BIG1 and BIG2 caused loss of clathrin adaptor proteins and redistribution of several TGN markers, but had no impact on COPI and several Golgi markers. Surprisingly, BIGs knockdown prevented neither traffic of VSVGtsO45 to the plasma membrane nor assembly of a polarized Golgi stack. Our observations indicate that COPII is the only coat required for sorting and export from the ER exit sites, while GBF1 but not BIGs, is required for COPI recruitment, Golgi subcompartmentalization and cargo progression to the cell surface.

Address correspondence to: Paul Melançon (Paul.Melancon{at}UAlberta.ca)






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