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

A Hausser, P Storz, S Märtens, G Link, A Toker… - Nature cell …, 2005 - nature.com
A Hausser, P Storz, S Märtens, G Link, A Toker, K Pfizenmaier
Nature cell biology, 2005nature.com
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 …
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.
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