Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIβ at the Golgi complex

Angelika Hausser, Peter Storz, Susanne Märtens, Gisela Link, Alex Toker, Klaus Pfizenmaier

Research output: Contribution to journalArticlepeer-review

255 Scopus citations

Abstract

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

Original languageEnglish (US)
Pages (from-to)880-886
Number of pages7
JournalNature Cell Biology
Volume7
Issue number9
DOIs
StatePublished - Sep 2005

ASJC Scopus subject areas

  • Cell Biology

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