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Originally published In Press as doi:10.1074/jbc.M003213200 on June 5, 2000

J. Biol. Chem., Vol. 275, Issue 33, 25342-25350, August 18, 2000
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beta 2-Adrenergic Receptor Activates Extracellular Signal-regulated Kinases (ERKs) via the Small G Protein Rap1 and the Serine/Threonine Kinase B-Raf*

John M. Schmitt and Philip J. S. StorkDagger

From the Vollum Institute and the Department of Cell and Developmental Biology, Oregon Health Sciences University, Portland, Oregon 97201

G protein-coupled receptors can induce cellular proliferation by stimulating the mitogen-activated protein (MAP) kinase cascade. Heterotrimeric G proteins are composed of both alpha  and beta gamma subunits that can signal independently to diverse intracellular signaling pathways including those that activate MAP kinases. In this study, we examined the ability of isoproterenol, an agonist of the beta 2-adrenergic receptor (beta 2AR), to stimulate extracellular signal-regulated kinases (ERKs). Using HEK293 cells, which express endogenous beta 2AR, we show that isoproterenol stimulates ERKs via beta 2AR. This action of isoproterenol requires cAMP-dependent protein kinase and is insensitive to pertussis toxin, suggesting that Galpha s activation of cAMP-dependent protein kinase is required. Interestingly, beta 2AR activates both the small G proteins Rap1 and Ras, but only Rap1 is capable of coupling to Raf isoforms. beta 2AR inhibits the Ras-dependent activation of both Raf isoforms Raf-1 and B-Raf, whereas Rap1 activation by isoproterenol recruits and activates B-Raf. beta 2AR activation of ERKs is not blocked by expression of RasN17, an interfering mutant of Ras, but is blocked by expression of either RapN17 or Rap1GAP1, both of which interfere with Rap1 signaling. We propose that isoproterenol can activate ERKs via Rap1 and B-Raf in these cells.

* 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 To whom correspondence should be addressed: Vollum Inst., L474, Oregon Health Sciences University, 3181 S.W. Sam Jackson Park Rd., Portland, OR 97201-3098. Tel.: 503-494-5494; E-mail: stork@ohsu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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