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Sci. STKE, 18 September 2001
Vol. 2001, Issue 100, p. re12
[DOI: 10.1126/stke.2001.100.re12]

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Judging a Protein by More Than Its Name: GSK-3

James R. Woodgett

The author is at the Ontario Cancer Institute within the Princess Margaret Hospital, 610 University Avenue, Toronto, Ontario, M5G 2M9 Canada. E-mail: jwoodget{at}oci.utoronto.ca

Abstract: As knowledge of cellular signal transduction has accumulated, general truisms have emerged, including the notion that signaling proteins are usually activated by stimuli and that they, in turn, mediate the actions of specific agonists. Glycogen synthase kinase-3 (GSK-3) is an unusual protein-serine kinase that bucks these conventions. This evolutionarily conserved protein kinase is active in resting cells and is inhibited in response to activation of several distinct pathways, including those acting by elevation of 3' phosphorylated phosphatidylinositol lipids and adenosine 3'-5'-monophosphate (cAMP). In addition, GSK-3 is distinctly regulated by, and is a core component of, the Wnt pathway. This review describes the unique characteristics of this decidedly oddball protein kinase in terms of its diverse biological functions, plethora of targets, role in several human diseases, and consequential potential as a therapeutic target.

Citation: J. R. Woodgett, Judging a Protein by More Than Its Name: GSK-3. Sci. STKE 2001, re12 (2001).

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