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J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.R800064-JLR200 on November 24, 2008

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Journal of Lipid Research, Vol. 50, S266-S271, April 2009
Copyright © 2009 by American Society for Biochemistry and Molecular Biology

Signaling

Lipid activation of protein kinases

Alexandra C. Newton1

Department of Pharmacology, University of California at San Diego, La Jolla, CA 92093-0721

This work was supported in part by National Institutes of Health GM43154.

Published, JLR Papers in Press, November 24, 2008.

1 To whom correspondence should be addressed. e-mail: anewton{at}ucsd.edu


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.

Supplementary key words protein kinase C • Akt • diacylglycerol • phosphatidylinositol-3,4,5-tris phosphate

Abbreviations: AGC kinases, protein kinases A, G and C; PDK-1, phosphoinositide-dependent kinase-1; PH, pleckstrin homology; PHLPP, PH domain Leucine-rich repeat protein phosphatase; PIP3, phosphatidylinositol-3,4,5-trisphosphate; PKC, protein kinase C; PX, phox


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JLR 50th Anniversary Collections
Anniversary Collection::Signaling

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