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Originally published In Press as doi:10.1074/jbc.M100914200 on March 26, 2001

J. Biol. Chem., Vol. 276, Issue 28, 25672-25679, July 13, 2001
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Galpha Minigenes Expressing C-terminal Peptides Serve as Specific Inhibitors of Thrombin-mediated Endothelial Activation*

Annette GilchristDagger ||, Jurgen F. VanhauweDagger , Anli LiDagger , Tarita O. ThomasDagger , Tatyana Voyno-Yasenetskaya§, and Heidi E. HammDagger §||

From the Dagger  Institute for Neuroscience and the || Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Chicago, Illinois 60611 and the § Department of Pharmacology, University of Illinois at Chicago, Chicago, Illinois 60610

The C termini of G protein alpha  subunits are critical for binding to their cognate receptors, and peptides corresponding to the C terminus can serve as competitive inhibitors of G protein-coupled receptor-G protein interactions. This interface is quite specific as a single amino acid difference annuls the ability of a Galpha i peptide to bind the A1 adenosine receptor (Gilchrist, A., Mazzoni, M., Dineen, B., Dice, A., Linden, J., Dunwiddie, T., and Hamm, H. E. (1998 ) J. Biol. Chem. 273, 14912-14919). Recently, we demonstrated that a plasmid minigene vector encoding the C-terminal sequence of Galpha i could specifically inhibit downstream responses to agonist stimulation of the muscarinic M2 receptor (Gilchrist, A., Bunemann, M., Li, A., Hosey, M. M., and H. E. Hamm (1999) J. Biol. Chem. 274, 6610-6616). To selectively antagonize G protein signal transduction events and determine which G protein underlies a given thrombin-induced response, we generated minigene vectors that encode the C-terminal sequence for each family of Galpha subunits. Minigene vectors expressing Galpha C-terminal peptides (Galpha i, Galpha q, Galpha 12, and Galpha 13) or the control minigene vector, which expresses the Galpha i peptide in random order (GiR), were systematically introduced into a human microvascular endothelial cell line. The C-terminal peptides serve as competitive inhibitors presumably by blocking the site on the G protein-coupled receptor that normally binds the G protein. Our results not only confirm that each G protein can control certain signaling events, they emphasize the specificity of the G protein-coupled receptor-G protein interface. In addition, the C-terminal Galpha minigenes appear to be a powerful tool for dissecting out the G protein that mediates a given physiological function following thrombin activation.

* This work was supported by Grant HL60678-01A1 (to A. G., T. V-Y., and H. E. H.) from the National Institutes of Health.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.

To whom correspondence should be addressed: Dept. of Pharmacology, Vanderbilt University Medical Center, 442 Robinson Research Bldg., 23rd and Pierce Dr., Nashville, TN 37232. Tel.: 615-343-3533; Fax: 615-343-1084; E-mail: heidi.hamm@mcmail.vanderbilt.edu.

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