GBF1: A Novel Golgi-associated BFA-resistant Guanine Nucleotide Exchange Factor That Displays Specificity for ADP-ribosylation Factor 5

doi:10.1083/jcb.146.1.71

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J. Cell Biol., Volume 146, Number 1, July 12, 1999 71-84
Copyright © 1999 by The Rockefeller University Press.

GBF1: A Novel Golgi-associated BFA-resistant Guanine Nucleotide Exchange Factor That Displays Specificity for ADP-ribosylation Factor 5

Alejandro Claude^a, Bao-Ping Zhao^a, Craig E. Kuziemsky^a, Sophie Dahan^b, Scott J. Berger^c, Jian-Ping Yan^c, Adrian D. Armold^c, Eric M. Sullivan^c, and Paul Melançon^a
^a Department of Cell Biology, University of Alberta, Edmonton, Alberta, Canada, T6G 2H7
^b Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada, H3A 2B2
^c Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309

Expression cloning from a cDNA library prepared from a mutantCHO cell line with Golgi-specific resistance to Brefeldin A(BFA) identified a novel 206-kD protein with a Sec7 domain termedGBF1 for Golgi BFA resistance factor 1. Overexpression of GBF1allowed transfected cells to maintain normal Golgi morphologyand grow in the presence of BFA. Golgi- enriched membrane fractionsfrom such transfected cells displayed normal levels of ADP ribosylationfactors (ARFs) activation and coat protein recruitment thatwere, however, BFA resistant. Hexahistidine-tagged–GBF1exhibited BFA-resistant guanine nucleotide exchange activitythat appears specific towards ARF5 at physiological Mg²⁺concentration.Characterization of cDNAs recovered from the mutant and wild-typeparental lines established that transcripts in these cells hadidentical sequence and, therefore, that GBF1 was naturally BFAresistant. GBF1 was primarily cytosolic but a significant poolcolocalized to a perinuclear structure with the ß-subunitof COPI. Immunogold labeling showed highest density of GBF1over Golgi cisternae and significant labeling over pleiomorphicsmooth vesiculotubular structures. The BFA-resistant natureof GBF1 suggests involvement in retrograde traffic.

Key Words: Golgi complex, Brefeldin A, Sec7, ADP-ribosylation factor, proteintraffic

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