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

Nat Cell Biol. 2005 Sep;7(9):880-6. doi: 10.1038/ncb1289. Epub 2005 Aug 14.


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

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 1-Phosphatidylinositol 4-Kinase / metabolism*
  • Amino Acid Motifs / physiology
  • Animals
  • Biological Transport, Active / physiology
  • COS Cells
  • Cell Membrane / enzymology
  • Chlorocebus aethiops*
  • Conserved Sequence / physiology
  • Enzyme Activation / physiology
  • Evolution, Molecular
  • Golgi Apparatus / enzymology*
  • Golgi Apparatus / metabolism
  • Humans
  • Lipid Metabolism
  • Membrane Glycoproteins / metabolism
  • Phosphorylation
  • Protein Isoforms / metabolism
  • Protein Kinase C / metabolism*
  • Transport Vesicles / enzymology*
  • Viral Envelope Proteins / metabolism


  • G protein, vesicular stomatitis virus
  • Membrane Glycoproteins
  • Protein Isoforms
  • Viral Envelope Proteins
  • 1-Phosphatidylinositol 4-Kinase
  • protein kinase D
  • Protein Kinase C