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

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 o...

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Bibliographic Details
Published in:Cell Vol. 65; no. 4; p. 663
Main Authors: Boulton, Teri G, Nye, Steven H, Robbins, David J, Ip, Nancy Y, Radziejewska, Elizabeth, Morgenbesser, Sharon D, DePinho, Ronald A, Panayotatos, Nikos, Cobb, Melanie H, Yancopoulos, George D
Format: Journal Article
Language:English
Published: United States 17-05-1991
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Summary: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.
ISSN:0092-8674
DOI:10.1016/0092-8674(91)90098-J