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Catalytic Activation of the Phosphatase MKP-3 by ERK2 Mitogen-Activated Protein Kinase

Montserrat Camps, Anthony Nichols, Corine Gillieron, Bruno Antonsson, Marco Muda, Christian Chabert, Ursula Boschert and Steve Arkinstall
Science
New Series, Vol. 280, No. 5367 (May 22, 1998), pp. 1262-1265
Stable URL: http://www.jstor.org/stable/2896074
Page Count: 4
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Catalytic Activation of the Phosphatase MKP-3 by ERK2 Mitogen-Activated Protein Kinase
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Abstract

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 kinases bound MKP-3 or caused its catalytic activation. These kinases were also resistant to enzymatic inactivation by MKP-3. Another homologous but nonselective phosphatase, MKP-4, bound and was activated by ERK2, JNK/SAPK, and p38 MAP kinases. Catalytic activation of MAP kinase phosphatases through substrate binding may regulate MAP kinase activation by a large number of receptor systems.

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