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Vol. 16, Issue 2, 776-793, February 2005
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* Department of Cellular and Molecular Medicine and the Howard Hughes Medical Institute, School of Medicine, University of California at San Diego, La Jolla, CA 92093-0668;
Banting and Best Department of Medical Research and Department of Medical Genetics and Microbiology, University of Toronto, Toronto, Ontario, Canada M5G 1L6; and
Department of Biological Sciences, Laboratory for Molecular Biology, University of Illinois at Chicago, Chicago, IL 60607
Submitted August 13, 2004;
Accepted November 19, 2004
Monitoring Editor: Randy Schekman
Phosphorylated derivatives of phosphatidylinositol are essential regulators of both endocytic and exocytic trafficking in eukaryotic cells. In Saccharomyces cerevisiae, the phosphatidylinositol 4-kinase, Pik1p generates a distinct pool of PtdIns(4)P that is required for normal Golgi structure and secretory function. Here, we utilize a synthetic genetic array analysis of a conditional pik1 mutant to identify candidate components of the Pik1p/PtdIns(4)P signaling pathway at the Golgi. Our data suggest a mechanistic involvement for Pik1p with a specific subset of Golgi-associated proteins, including the Ypt31p rab-GTPase and the TRAPPII protein complex, to regulate protein trafficking through the secretory pathway. We further demonstrate that TRAPPII specifically functions in a Ypt31p-dependent pathway and identify Gyp2p as the first biologically relevant GTPase activating protein for Ypt31p. We propose that multiple stage-specific signals, which may include Pik1p/PtdIns(4)P, TRAPPII and Gyp2p, impinge upon Ypt31 signaling to regulate Golgi secretory function.
Abbreviations used: CPY, carboxypeptidase Y; GAP, GTPase-activating protein; GFP, green fluorescent protein; PtdIns(4)P, phosphatidylinositol 4-phosphate; PtdIns(4,5)P2, phosphatidylinositol 4,5 bisphosphate; PH, pleckstrin homology; TRAPP, transport protein particle.
The online version of this article contains supplemental material on MBC Online (http://www.molbiolcell.org).
Corresponding author. E-mail address: semr{at}ucsd.edu.
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