Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase.

  title={Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase.},
  author={Montserrat Camps and Anthony C Nichols and Corine Gilli{\'e}ron and Bruno Antonsson and M. Hilmi Muda and Christian Chabert and Ursula Boschert and Steve Arkinstall},
  volume={280 5367},
MAP kinase phosphatase-3 (MKP-3) dephosphorylates phosphotyrosine and phosphothreonine and inactivates selectively ERK family mitogen-activated protein (MAP) kinases. MKP-3 was activated by direct binding to purified ERK2. Activation was independent of protein kinase activity and required binding of ERK2 to the noncatalytic amino-terminus of MKP-3. Neither the gain-of-function Sevenmaker ERK2 mutant D319N nor c-Jun amino-terminal kinase-stress-activated protein kinase (JNK/SAPK) or p38 MAP… CONTINUE READING
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Cell 75, 487 (1993); S

  • H. Sun, C. H. Charles, L. F. Lau, N. K. Tonks
  • M. Keyse, Biochim. Biophys. Acta
  • 1265

Science 258, 478 (1992); J

  • C. M. Crews, A. Alessandrini, R. L. Erikson
  • Wu et al., Proc. Natl. Acad. Sci. U.S.A. 90, 173…
  • 1143

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