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Papers In Press, published online ahead of print November 9, 2001
J. Biol. Chem, 10.1074/jbc.M108571200
Submitted on September 6, 2001
Revised on November 1, 2001
Accepted on November 9, 2001

Multiple roles for phosphatidylinositol 4-kinase in biosynthetic transport in polarized MDCK cells

Jennifer R. Bruns, Mark A. Ellis, Andreas Jeromin, and Ora A. Weisz

Renal-Electrolyte Division, University of Pittsburgh, Pittsburgh, PA 15261

Corresponding Author: weisz{at}msx.dept-med.pitt.edu

Phosphatidylinositols (PI) play important roles in regulating numerous cellular processes including cytoskeletal organization and membrane trafficking. The control of PI metabolism by phosphatidylinositol kinases (PIKs) has been the subject of extensive investigation; however, little is known about how phosphatidylinositol kinases regulate traffic in polarized epithelial cells. Because PI4K-mediated phosphatidylinositol 4-phosphate [PI(4)P] production has been suggested to regulate biosynthetic traffic in yeast and mammalian cells, we have examined the role of PI4Kbeta in protein delivery in polarized MDCK cells, at different levels of the biosynthetic pathway. Expression of wild type PI4Kbeta had no effect on the rate of transport of influenza hemagglutinin (HA) through the Golgi complex, but inhibited the rate of TGN-to-cell surface delivery of this protein. By contrast, expression of dominant-negative, kinase dead PI4Kbeta (PI4Kbeta D656A) inhibited intra-Golgi transport but stimulated TGN-to-cell surface delivery of HA. Moreover, expression of PI4Kbeta D656A significantly increased the solubility in cold Triton X-100 of HA staged in the TGN, suggesting that altered association of HA with lipid rafts may be responsible for the enhanced transport rate. Both wild type and kinase dead PI4Kbeta inhibited basolateral delivery of vesicular stomatitis virus G protein, suggesting an effector function for PI4Kbeta in the regulation of basolateral traffic. Thus, by contrast with the observed requirement for PI4K activity and PI(4)P for efficient transport in yeast, our data suggest that changes in PI(4)P levels can stimulate and inhibit Golgi to cell surface delivery in mammalian cells.


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