An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control

Teri G. Boulton, George D. Yancopoulos, Jill S. Gregory, Clive A. Slaughter, Carolyn Moomaw, Joan Hsu, Melanie H. Cobb

Research output: Contribution to journalArticlepeer-review

601 Scopus citations

Abstract

A protein kinase characterized by its ability to phosphorylate microtubule-associated protein-2 (MAP2), is thought to be an early intermediate in an insulin-stimulated phosphorylation cascade and in a variety of other mammalian cell responses to extracellular signals. A complementary DNA that encodes this protein serine-threonine kinase has been cloned, and the protein designated extracellular signal-regulated kinase 1 (ERK1). ERK1 has striking similarity to two protein kinases, KSS1 and FUS3, from yeast. The yeast kinases function in an antagonistic manner to regulate the cell cycle in response to mating factors. Thus, ERK1 and the two yeast kinases constitute a family of evolutionarily conserved enzymes involved in regulating the response of eukaryotic cells to extracellular signals.

Original languageEnglish (US)
Pages (from-to)64-67
Number of pages4
JournalScience
Volume249
Issue number4964
StatePublished - 1990
Externally publishedYes

ASJC Scopus subject areas

  • General

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