Negative regulation of MAPKK by phosphorylation of a conserved serine residue equivalent to Ser212 of MEK1.

@article{Gopalbhai2003NegativeRO,
  title={Negative regulation of MAPKK by phosphorylation of a conserved serine residue equivalent to Ser212 of MEK1.},
  author={Kailesh Gopalbhai and Gregor Jansen and Genevi{\`e}ve Beauregard and Malcolm Whiteway and France Dumas and Cunle Wu and Sylvain Meloche},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 10},
  pages={8118-25}
}
The MAPKKs MEK1 and MEK2 are activated by phosphorylation, but little is known about how these enzymes are inactivated. Here, we show that MEK1 is phosphorylated in vivo at Ser(212), a residue conserved among all MAPKK family members. Mutation of Ser(212) to alanine enhanced the basal activity of MEK1, whereas the phosphomimetic aspartate mutation completely suppressed the activation of both wild-type MEK1 and the constitutively activated MEK1(S218D/S222D) mutant. Phosphorylation of Ser(212… CONTINUE READING

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