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A more recent version of this article appeared on January 1, 2002
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Submitted on August 23, 2001
Revised on October 24, 2001
Accepted on October 26, 2001
1 Department of Cell Biology, University of Alberta, Edmonton, Alberta, Canada
2 Department of Cell Biology, University of Alberta, MSB 5-14, Edmonton, Alberta T6G 2H7, Canada
* Corresponding author. E-mail address: Paul.Melancon{at}ualberta.ca.
Activation of several ADP-ribosylation factors (ARFs) by guanine nucleotide exchange factors (GEFs) regulates recruitment of coat proteins on the Golgi complex and is generally assumed to be the target of brefeldin A (BFA). The large ARF-GEFs, GBF1 and BIGs, all localize to this organelle but catalyze exchange preferentially on Class II and Class I ARFs, respectively. We now demonstrate using quantitative confocal microscopy that these GEFs show a very limited overlap (15 and 23%). In contrast, GBF1 co-localizes with the cis-marker p115 (81 and 86%) while BIGs overlap extensively with TGN38 (83 and 92%). Consistent with these distributions, GBF1, but not BIG1, partially relocalized to peripheral sites following incubation at 15°C. The new GBF1 structures represent peripheral vesiculo-tubular clusters (VTCs), since 88% of structures analyzed stained for both GBF1 and p115. Furthermore, as expected of VTCs, they rapidly re-clustered to the Golgi complex in a microtubule-dependent manner upon warm-up. These observations suggest that GBF1 and BIGs activate distinct subclasses of ARFs in specific locations to regulate different types of reactions. In agreement with this possibility, the COPI coat overlapped to a greater extent with GBF1 (64%) than BIG1 (31%), while clathrin showed limited overlap with BIG1, and virtually none with GBF1.
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