ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF

Teri G. Boulton, Steven H. Nye, David J. Robbins, Nancy Y. Ip, Elizabeth Radzlejewska, Sharon D. Morgenbesser, Ronald A. DePinho, Nikos Panayotatos, Melanie H. Cobb, George D. Yancopoulos

Research output: Contribution to journalArticlepeer-review

1706 Scopus citations

Abstract

We recently described the purification and cloning of extracellular signal-regulated kinase 1 (ERK1), which appears to play a pivotal role in converting tyrosine phosphorylation into the serine/threonine phosphorylations that regulate downstream events. We now describe cloning and characterization of two ERK1-related kinases, ERK2 and ERK3, and provide evidence suggesting that there are additional ERK family members. At least two of the ERKs are activated in response to growth factors; their activations correlate with tyrosine phophorylation, but also depend on additional modifications. Transcripts corresponding to the three cloned ERKs are distinctly regulated both in vivo and in a differentiating cell line. Thus, this family of kinases may serve as intermediates that depend on tyrosine phosphorylation to activate serine/threonine phosphorylation cascades. Individual family members may mediate responses in different developmental stages, in different cell types, or following exposure to different extracellular signals.

Original languageEnglish (US)
Pages (from-to)663-675
Number of pages13
JournalCell
Volume65
Issue number4
DOIs
StatePublished - May 17 1991

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology

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