Lipid activation of protein kinases

J Lipid Res. 2009 Apr;50 Suppl(Suppl):S266-71. doi: 10.1194/jlr.R800064-JLR200. Epub 2008 Nov 24.

Abstract

Lipids acutely control the amplitude, duration, and subcellular location of signaling by lipid second messenger-responsive kinases. Typically, this activation is controlled by membrane-targeting modules that allosterically control the function of kinase domains within the same polypeptide. Protein kinase C (PKC) has served as the archetypal lipid-regulated kinase, providing a prototype for lipid-controlled kinase activation that is followed by kinases throughout the kinome, including its close cousin, Akt (protein kinase B). This review addresses the molecular mechanisms by which PKC and Akt transduce signals propagated by the two major lipid second messenger pathways in cells, those of diacylglycerol signaling and phosphatidylinositol-3,4,5-trisphosphate (PIP3) signaling, respectively.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Cell Membrane / enzymology
  • Enzyme Activation
  • Lipid Metabolism*
  • Protein Kinases / metabolism*
  • Signal Transduction

Substances

  • Protein Kinases