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

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.

journal_name

Cell

journal_title

Cell

authors

Boulton TG,Nye SH,Robbins DJ,Ip NY,Radziejewska E,Morgenbesser SD,DePinho RA,Panayotatos N,Cobb MH,Yancopoulos GD

doi

10.1016/0092-8674(91)90098-j

subject

Has Abstract

pub_date

1991-05-17 00:00:00

pages

663-75

issue

4

eissn

0092-8674

issn

1097-4172

pii

0092-8674(91)90098-J

journal_volume

65

pub_type

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