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
Celljournal_title
Cellauthors
Boulton TG,Nye SH,Robbins DJ,Ip NY,Radziejewska E,Morgenbesser SD,DePinho RA,Panayotatos N,Cobb MH,Yancopoulos GDdoi
10.1016/0092-8674(91)90098-jsubject
Has Abstractpub_date
1991-05-17 00:00:00pages
663-75issue
4eissn
0092-8674issn
1097-4172pii
0092-8674(91)90098-Jjournal_volume
65pub_type
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