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

Authors Boulton, T.G.
Nye, S.H.
Robbins, D.J.
Ip, N.Y. View this author's profile
Radziejewska, E.
Morgenbesser, S.D.
DePinho, R.A.
Panayotatos, N.
Cobb, M.H.
Yancopoulos, G.D.
Issue Date 1991
Source Cell , v. 65, (4), 1991, p. 663-675
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 phosphorylation, 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
Language English
Format Article
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