Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

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

Abstract: 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).

Read the Full Text


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882