Lipid activation of protein kinases.
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.
Newton
Alexandra C
AC
Department of Pharmacology, University of California at San Diego, La Jolla, CA 92093-0721, USA. anewton@ucsd.edu
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004789:Enzyme Activation; D050356:Lipid Metabolism; D011494:Protein Kinases / Q000378:metabolism*; D015398:Signal Transduction
D011494:Protein Kinases