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

doi:10.1038/ncb1289

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

Cancer Biology

Research output: Contribution to journal › Article › peer-review

259 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 language	English (US)
Pages (from-to)	880-886
Number of pages	7
Journal	Nature Cell Biology
Volume	7
Issue number	9
DOIs	https://doi.org/10.1038/ncb1289
State	Published - Sep 2005

ASJC Scopus subject areas

Cell Biology

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

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.",

author = "Angelika Hausser and Peter Storz and Susanne M{\"a}rtens and Gisela Link and Alex Toker and Klaus Pfizenmaier",

note = "Funding Information: We wish to thank L. Rameh for help with the lipid-kinase assay, and E. Behrle and O. Selchow for help with the confocal microscopy. This work was supported by grants from the Deutsche Forschungsgemeinschaft (SFB 495 to K.P.), the Landesstiftung Baden-W{\"u}rttemberg (to A.H.) and from the National Institutes of Health (CA075134 to A.T.).",

year = "2005",

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doi = "10.1038/ncb1289",

language = "English (US)",

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pages = "880--886",

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T1 - Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIβ at the Golgi complex

AU - Hausser, Angelika

AU - Storz, Peter

AU - Märtens, Susanne

AU - Link, Gisela

AU - Toker, Alex

AU - Pfizenmaier, Klaus

N1 - Funding Information: We wish to thank L. Rameh for help with the lipid-kinase assay, and E. Behrle and O. Selchow for help with the confocal microscopy. This work was supported by grants from the Deutsche Forschungsgemeinschaft (SFB 495 to K.P.), the Landesstiftung Baden-Württemberg (to A.H.) and from the National Institutes of Health (CA075134 to A.T.).

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N2 - 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.

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

Abstract

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