A novel mitogen-activated protein kinase phosphatase: Structure, expression, and regulation

Anita Misra-Press, Caroline S. Rim, Hong Yao, Mark S. Roberson, Philip J.S. Stork

Research output: Contribution to journalArticlepeer-review

217 Scopus citations

Abstract

Mitogen-activated protein (MAP) kinase lies at the convergence of various extracellular ligand-mediated signaling pathways. It is activated by the dual-specificity kinase, MAP kinase kinase or MEK. MAP kinase inactivation is mediated by dephosphorylation via specific MAP kinase phosphatases (MKPs). One MKP (MKP-1 (also known as 3CH134, Erp, or CL100)) has been reported to be expressed in a wide range of tissues and cells. We report the identification of a second widely expressed MKP, termed MKP-2, isolated from PC12 cells. MKP-2 showed significant homology with MKP-1 (58.8% at the amino acid level) and, like MKP-1, displayed vanadate-sensitive phosphatase activity against MAP kinase in vitro. Overexpression of MKP-2 in vivo inhibited MAP kinase-dependent gene transcription in PC12 cells. MKP-2 differed from MKP-1 in its tissue distribution and in its extent of induction by growth factors and agents that induce cellular stress, suggesting that these MKPs may have distinct physiological functions.

Original languageEnglish (US)
Pages (from-to)14587-14596
Number of pages10
JournalJournal of Biological Chemistry
Volume270
Issue number24
DOIs
StatePublished - Jun 16 1995

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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