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A more recent version of this article appeared on February 28, 2003
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M211870200v1
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Papers In Press, published online ahead of print December 27, 2002
J. Biol. Chem, 10.1074/jbc.M211870200
Submitted on November 21, 2002
Revised on December 20, 2002
Accepted on December 27, 2002

Negative regulation of MAP kinase kinases by phosphorylation of a conserved serine residue equivalent to Ser212 of MEK1

Kailesh Gopalbhai, Gregor Jansen, Geneviève Beauregard, Malcolm Whiteway, France Dumas, Cunle Wu, and Sylvain Meloche

Institut de recherches cliniques de Montréal, Montreal, Quebec H2W 1R7

Corresponding Author: melochs{at}ircm.qc.ca

The MAP kinase kinases (MAPKKs) MEK1/2 are activated by phosphorylation but little is known on how these enzymes are inactivated. Here we show that MEK1 is phosphorylated in vivo on Ser212, a residue conserved among all MAPKK family members. Mutation of Ser212 to alanine enhances the basal activity of MEK1, whereas the phospho-mimetic aspartate mutation completely suppresses the activation of both wild-type and constitutively-activated MEK1(S218D/S222D) mutant. Phosphorylation of Ser212 does not interfere with the activating phosphorylation of MEK1 on Ser218/Ser222 or with binding to ERK2 substrate. Importantly, mimicking phosphorylation of the equivalent Ser212 residue of yeast MAPKKs Pbs2p and Ste7p similarly abrogates their biological function. Our findings suggest that Ser212 phosphorylation represents an evolutionarily conserved mechanism involved in the negative regulation of MAPKKs.


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