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A more recent version of this article appeared on December 6, 2002
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Papers In Press, published online ahead of print September 23, 2002
J. Biol. Chem, 10.1074/jbc.M208535200
Submitted on August 20, 2002
Revised on September 23, 2002
Accepted on September 23, 2002

Cell condition-dependent regulation of ERK5 by cAMP

Gray W. Pearson and Melanie H. Cobb

Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9041

Corresponding Author: mcobb{at}mednet.swmed.edu

ERK5 activity is increased by agents known to activate receptor tyrosine kinases, G-protein coupled receptors and stress response pathways. We now find a role for cAMP in the regulation of ERK5. ERK5 is activated by forskolin, isoproterenol and epinephrine in NIH3T3 cells and C2C12 myoblasts. ERK1/2 are also activated by cAMP in NIH3T3 cells, but not in C2C12 myoblasts, demonstrating differential regulation of ERK5 and ERK1/2 by cAMP. We examined the effect of cell context on activation of ERK5 and discovered ERK5 activity is inhibited, rather than activated, by cAMP in confluent, serum-deprived NIH3T3 cells and C2C12 myoblasts. Our results suggest that regulation of MAP kinase pathways by cAMP is not only dictated by cell type, but also by cell context.


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