Abstract
Protein kinase D (PKD) regulates the fission of vesicles originating from the trans-Golgi network. We show that phosphatidylinositol 4-kinase IIIbeta (PI4KIIIbeta) - 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 PI4KIIIbeta at a motif that is highly conserved from yeast to humans. PKD-mediated phosphorylation stimulated lipid kinase activity of PI4KIIIbeta and enhanced vesicular stomatitis virus G-protein transport to the plasma membrane. The identification of PI4KIIIbeta as one of the PKD substrates should help to reveal the molecular events that enable transport-carrier formation.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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1-Phosphatidylinositol 4-Kinase / metabolism*
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Amino Acid Motifs / physiology
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Animals
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Biological Transport, Active / physiology
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COS Cells
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Cell Membrane / enzymology
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Chlorocebus aethiops*
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Conserved Sequence / physiology
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Enzyme Activation / physiology
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Evolution, Molecular
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Golgi Apparatus / enzymology*
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Golgi Apparatus / metabolism
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Humans
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Lipid Metabolism
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Membrane Glycoproteins / metabolism
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Phosphorylation
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Protein Isoforms / metabolism
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Protein Kinase C / metabolism*
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Transport Vesicles / enzymology*
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Viral Envelope Proteins / metabolism
Substances
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G protein, vesicular stomatitis virus
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Membrane Glycoproteins
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Protein Isoforms
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Viral Envelope Proteins
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1-Phosphatidylinositol 4-Kinase
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protein kinase D
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Protein Kinase C