Sci. STKE, 28 September 1999
Vol. 1999, Issue 1, p. pe1
[DOI: 10.1126/stke.1999.1.pe1]
PERSPECTIVES
Signal Transduction by MAP Kinases: Regulation by Phosphorylation-Dependent Switches
Alan J. Whitmarsh and
Roger J. Davis
The authors are at the Howard Hughes Medical Institute and Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605 USA. E-mail: roger.davis{at}umassmed.edu
Summary:
The kinases of mitogen-activated protein (MAP) kinase cascades transmit signals through sequential phosphorylation and activation of the enzymes. However, recent evidence indicates that protein-protein interactions between the kinases themselves or with substrates or other components are also a critical means of regulation. Whitmarsh and Davis summarize these findings with emphasis on new evidence from yeast that, when phosphorylated, a MAP kinase kinase actually switches from a negative regulator that binds to and inhibits its target MAP kinase to a positive regulator of that same enzyme.
Citation: A. J. Whitmarsh, R. J. Davis, Signal Transduction by MAP Kinases: Regulation by Phosphorylation-Dependent Switches. Sci. STKE 1999, pe1 (1999).
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