Protein kinase D (PKD) regulates the fission of vesicles from the trans-Golgi-network 1,2 . We show that phosphatidylinositol-4-kinase III beta (PI4KIIIβ), a key player in Golgi complex structure and function 3 , is a physiological substrate of PKD. Of the three PKD isoforms, only PKD1 and PKD2 phosphorylated PI4KIIIβ at a motif highly conserved from yeast to man. PKD mediated phosphorylation stimulated lipid kinase activity of PI4KIIIβ and enhanced VSV-G transport to plasma membrane. The identification of PI4KIIIβ as one of the PKD substrates should help to reveal the molecular events leading to transport carrier formation.
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