Author: ["Angelika Hausser","Peter Storz","Susanne Märtens","Gisela Link","Alex Toker","Klaus Pfizenmaier"]
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Abstract
Protein kinase D (PKD) regulates the fission of vesicles originating from the trans-Golgi network1,2. We show that phosphatidylinositol 4-kinase IIIβ (PI4KIIIβ) — 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 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.Cite this article
Hausser, A., Storz, P., Märtens, S. et al. Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIβ at the Golgi complex. Nat Cell Biol 7, 880–886 (2005). https://doi.org/10.1038/ncb1289 