Phosphorylation of MAP kinases by MAP/ERK involves multiple regions of MAP kinases

Research output: Contribution to journalArticle

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Abstract

Mitogen-activated protein (MAP) kinases are activated with great specificity by MAP/ERK kinases (MEKs). The basis for the specific activation is not understood. In this study chimeras composed of two MAP kinases, extracellular signal-regulated protein kinase 2 and p38, were assayed in vitro for phosphorylation and activation by different MEK isoforms to probe the requirements for productive interaction of MAP kinases with MEKs. Experimental results and modeling support the conclusion that the specificity of MEK/MAP kinase phosphorylation results from multiple contacts, including surfaces in both the N- and C-terminal domains.

Original languageEnglish (US)
Pages (from-to)16988-16994
Number of pages7
JournalJournal of Biological Chemistry
Volume274
Issue number24
DOIs
StatePublished - Jun 11 1999

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Phosphorylation
Mitogen-Activated Protein Kinases
Mitogens
Mitogen-Activated Protein Kinase Kinases
Proteins
Chemical activation
Protein Kinases
Mitogen-Activated Protein Kinase 1
Protein Isoforms
Phosphotransferases

ASJC Scopus subject areas

  • Biochemistry

Cite this

Phosphorylation of MAP kinases by MAP/ERK involves multiple regions of MAP kinases. / Wilsbacher, Julie L.; Goldsmith, Elizabeth J.; Cobb, Melanie H.

In: Journal of Biological Chemistry, Vol. 274, No. 24, 11.06.1999, p. 16988-16994.

Research output: Contribution to journalArticle

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