Nature Cell Biology
7, 880 - 886 (2005)
Published online: 14 August 2005; | doi:10.1038/ncb1289
Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase III at the Golgi complexAngelika Hausser1, Peter Storz2, Susanne Märtens1, Gisela Link1, Alex Toker2
& Klaus Pfizenmaier11
Institute for Cell Biology and Immunology, University of Stuttgart, Allmandring 31, 70569 Stuttgart, Germany. 2
Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA.
Correspondence should be addressed to Angelika Hausser angelika.hausser@izi.uni-stuttgart.de or Klaus Pfizenmaier klaus.pfizenmaier@izi.uni-stuttgart.de Protein kinase D (PKD) regulates the fission of vesicles originating from the trans-Golgi network1,
2. We show that phosphatidylinositol 4-kinase III (PI4KIII) — a key player in the structure and function of the Golgi complex3 — is a physiological substrate of PKD. Of the three PKD isoforms, only PKD1 and PKD2 phosphorylated PI4KIII at a motif that is highly conserved from yeast to humans. PKD-mediated phosphorylation stimulated lipid kinase activity of PI4KIII and enhanced vesicular stomatitis virus G-protein transport to the plasma membrane. The identification of PI4KIII as one of the PKD substrates should help to reveal the molecular events that enable transport-carrier formation.
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