TY - JOUR
T1 - ERKs
T2 - A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF
AU - Boulton, Teri G.
AU - Nye, Steven H.
AU - Robbins, David J.
AU - Ip, Nancy Y.
AU - Radzlejewska, Elizabeth
AU - Morgenbesser, Sharon D.
AU - DePinho, Ronald A.
AU - Panayotatos, Nikos
AU - Cobb, Melanie H.
AU - Yancopoulos, George D.
N1 - Funding Information:
The authors would like to thank Leonard Schleifer, Alfred G. Gilman, Eric Shooter, Stephen P. Squinto, and the rest of the Ftegeneron community for encouragement and stimulating discussions. The authors also thank Natalie Ahn, Rony Seger, Edwin Krebs, and James Ferrell for communicating data prior to publication, John Rudge for help with astrocyte cultures, Leonardo Bellusci and Peter C. Maisonpierre for their help with the Northern analyses, Moses V. Chao for his LANGFR probe, Lloyd A. Greene for the PC12 cell line, Jill Gregory for early work on PC12 cells, Colleen Vanderbilt for Rat 1 HlRc B and PC12 culture, and Jo Hicks for preparation of the manuscript. This study is in partial fulfillment of the requirements for the Ph.D. degree in Molecular and Cell Biology at University of Texas at Dallas, Richardson, TX, for T. G. B., and in partial fulfillment of the requirements for the Ph.D. degree in Pharmacology at University of Texas Southwestern, Dallas, TX, for D. J. R. This work was supported by Regeneron Pharmaceuticals, Inc. and by grant DK 34128 and Research Career Development Award DK 01918 from the National Institutes of Health and American Cancer Society Institutional grant #IN-142 to M. H. C.
PY - 1991/5/17
Y1 - 1991/5/17
N2 - 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.
AB - 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.
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U2 - 10.1016/0092-8674(91)90098-J
DO - 10.1016/0092-8674(91)90098-J
M3 - Article
C2 - 2032290
AN - SCOPUS:0025823448
SN - 0092-8674
VL - 65
SP - 663
EP - 675
JO - Cell
JF - Cell
IS - 4
ER -