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J. Biol. Chem., Vol. 277, Issue 50, 48094-48098, December 13, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/50/48094    most recent M208535200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Pearson, G. W. Articles by Cobb, M. H. Search for Related Content PubMed PubMed Citation Articles by Pearson, G. W. Articles by Cobb, M. H. Social Bookmarking                      What's this?

Cell Condition-dependent Regulation of ERK5 by cAMP^*

Gray W. Pearson 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.

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