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J. Biol. Chem., Vol. 277, Issue 3, 2012-2018, January 18, 2002
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From the Phosphatidylinositols (PI) play important roles
in regulating numerous cellular processes including cytoskeletal
organization and membrane trafficking. The control of PI metabolism by
phosphatidylinositol kinases has been the subject of extensive
investigation; however, little is known about how phosphatidylinositol
kinases regulate traffic in polarized epithelial cells. Because
phosphatidylinositol 4-kinase (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 PI4K Laboratory of Epithelial Cell Biology,
Renal-Electrolyte Division, University of Pittsburgh, Pittsburgh,
Pennsylvania 15261 and the § Samuel Lunenfeld Research
Institute, Mount Sinai Hospital, Toronto,
Ontario M5G 1X5, Canada
in protein delivery in polarized MDCK cells, at
different levels of the biosynthetic pathway. Expression of wild type
PI4K had no effect on the rate of transport of influenza
hemagglutinin (HA) through the Golgi complex, but inhibited the rate of
trans-Golgi network (TGN)-to-cell surface delivery of this
protein. By contrast, expression of dominant-negative, kinase-dead
PI4K (PI4KD656A) inhibited intra-Golgi transport but
stimulated TGN-to-cell surface delivery of HA. Moreover, expression of
PI4KD656A 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 PI4K inhibited
basolateral delivery of vesicular stomatitis virus G protein,
suggesting an effector function for PI4K 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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