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Originally published In Press as doi:10.1074/jbc.M208535200 on September 23, 2002

J. Biol. Chem., Vol. 277, Issue 50, 48094-48098, December 13, 2002
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Cell Condition-dependent Regulation of ERK5 by cAMP*

Gray W. PearsonDagger and Melanie H. Cobb§

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

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.

* This work was supported by National Institutes of Health Grant DK34128 and Welch Foundation Grant I1243.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Supported by an NIGMS, National Institutes of Health, Predoctoral Training Grant in the pharmacological sciences. This work was done in partial fulfillment of the requirements for the Ph.D. degree.

§ To whom correspondence should be addressed: Dept. of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75390-9041. Tel.: 214-648-3627; Fax: 214-648-3811; E-mail: mcobb@mednet.swmed.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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