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A more recent version of this article appeared on September 1, 2002
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Submitted on February 8, 2002
Revised on April 15, 2002
Accepted on June 13, 2002
1 Department of Biochemistry and Molecular Biology, University of Minnesota Duluth School of Medicine, 10 University Drive, Duluth, MN 55812
2 Department of Biochemistry and Molecular Biology, University of Minnesota Duluth School of Medicine, 10 University Drive, Duluth, MN 55812 (present address: Institute of Paper Science and Technology, 500 10th Street, N.W., Atlanta, GA 30318-5794)
* Corresponding author. E-mail address: aboman{at}d.umn.edu.
GGA proteins facilitate distinct steps of post-Golgi traffic. Human and yeast GGA proteins are only ~25% identical, but all GGA proteins have four similar domains based on function and sequence homology. GGA proteins are most conserved in the region that interacts with ARF proteins. To analyze the role of ARF in GGA protein localization and function, we performed mutational analyses of both human and yeast GGAs. To our surprise, yeast and human GGAs differ in their requirement for ARF interaction. We describe a point mutation in both yeast and mammalian GGA proteins that eliminates binding to ARFs. In mammalian cells, this mutation disrupts the localization of human GGA proteins. Yeast Gga function was studied using an assay for CPY missorting and synthetic temperature sensitive lethality between GGAs and VPS27. Based on these assays, we conclude that non-Arf-binding yeast Gga mutants can function normally in membrane trafficking. Using GFP-tagged Gga1p, we show that Arf interaction is not required for Gga localization to the Golgi. Truncation analysis of Gga1p and Gga2p suggests that the N-terminal VHS domain and C-terminal hinge and ear domains play significant roles in yeast Gga protein localization and function. Together, our data suggest that yeast Gga proteins function to assemble a protein complex at the late Golgi to initiate proper sorting and transport of specific cargo. Whereas mammalian GGAs must interact with ARF to localize to and function at the Golgi, interaction between yeast Ggas and Arf plays a minor role in Gga localization and function.
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