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Published online 26 March 2002. doi:10.1083/jcb.200201037
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© The Rockefeller University Press, 0021-9525/2002/4/63 $5.00
The Journal of Cell Biology, Volume 157, Number 1, April 1, 2002 63-78

Article

 Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex

Xinmin Li1, Marcos P. Rivas1, Min Fang1, Jennifer Marchena2, Bharat Mehrotra3, Anu Chaudhary3, Li Feng3, Glenn D. Prestwich3 and Vytas A. Bankaitis2

1 Department of Cell Biology, University of Alabama at Birmingham, Birmingham, AL 35294
2 Department of Cell and Developmental Biology, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599
3 Department of Medicinal Chemistry, College of Pharmacy, University of Utah, Salt Lake City, UT 84112

Address correspondence to Vytas A. Bankaitis, Department of Cell and Developmental Biology, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7090. Tel.: (919) 962-9870. Fax: (919) 966-1856. E-mail: bktis{at}med.unc.edu

Oxysterol binding proteins (OSBPs) comprise a large conserved family of proteins in eukaryotes. Their ubiquity notwithstanding, the functional activities of these proteins remain unknown. Kes1p, one of seven members of the yeast OSBP family, negatively regulates Golgi complex secretory functions that are dependent on the action of the major yeast phosphatidylinositol/phosphatidylcholine Sec14p. We now demonstrate that Kes1p is a peripheral membrane protein of the yeast Golgi complex, that localization to the Golgi complex is required for Kes1p function in vivo, and that targeting of Kes1p to the Golgi complex requires binding to a phosphoinositide pool generated via the action of the Pik1p, but not the Stt4p, PtdIns 4-kinase. Localization of Kes1p to yeast Golgi region also requires function of a conserved motif found in all members of the OSBP family. Finally, we present evidence to suggest that Kes1p may regulate adenosine diphosphate-ribosylation factor (ARF) function in yeast, and that it may be through altered regulation of ARF that Kes1p interfaces with Sec14p in controlling Golgi region secretory function.

Key Words: Kes1p; phosphoinositides; yeast Golgi; Sec14p; ARF


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