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

@article{Camps1998CatalyticAO,
  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},
  journal={Science},
  year={1998},
  volume={280 5367},
  pages={1262-5}
}
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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