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Originally published In Press as doi:10.1074/jbc.M107191200 on September 28, 2001

J. Biol. Chem., Vol. 276, Issue 49, 45751-45754, December 7, 2001
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The Signal Transfer Regions of Galpha s*

Yibang Chen, Barney Yoo, Jay B. Lee, Gezhi Weng, and Ravi IyengarDagger

From the Department of Pharmacology, Mount Sinai School of Medicine, New York, New York 10029

The crystal structure of soluble functional fragments of adenylyl cyclase complexed with Galpha s and forskolin, shows three regions of Galpha s in direct contact with adenylyl cyclase. The functions of these three regions are not known. We tested synthetic peptides encoding these regions of Galpha s on the activities of full-length adenylyl cyclases 2 and 6. A peptide encoding the Switch II region (amino acids 222-247) stimulated both adenylyl cyclases 2- to 3-fold. Forskolin synergized the stimulation. Addition of peptides in the presence of activated Galpha s partially inhibited Galpha s stimulation. Corresponding Switch II region peptides from Galpha q and Galpha i did not stimulate adenylyl cyclase. A peptide encoding the Switch I region (amino acids 199-216) also stimulated AC2 and AC6. The stimulatory effects of the two peptides at saturating concentrations were non-additive. A peptide encoding the third contact region (amino acids 268-286) located in the alpha 3-beta 5 region, inhibits basal, forskolin, and Galpha s-stimulated enzymatic activities. Since this region in Galpha s interacts with both the central cytoplasmic loop and C-terminal tail of adenylyl cyclases this peptide may be involved in blocking interactions between these two domains. These functional data in conjunction with the available structural information suggest that Galpha s activation of adenylyl cyclase is a complex event where the alpha 3-beta 5 loop of Galpha s may bring together the central cytoplasmic loop and C-terminal tail of adenylyl cyclase thus allowing the Switch I and Switch II regions to function as signal transfer regions to activate adenylyl cyclase.

* This research was supported by National Institutes of Health Grant DK-38761.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: Dept. of Pharmacology, Box 1215, Mount Sinai School of Medicine, One Gustave Levy Place, New York, NY 10029. Tel.: 212-659-1707; Fax: 212-831-0114; E-mail: ravi.iyengar@mssm.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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