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Volume 272, Number 11, Issue of March 14, 1997 pp. 6898-6902
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

The Thrombin Receptor Second Cytoplasmic Loop Confers Coupling to Gq-like G Proteins in Chimeric Receptors
ADDITIONAL EVIDENCE FOR A COMMON TRANSMEMBRANE SIGNALING AND G PROTEIN COUPLING MECHANISM IN G PROTEIN-COUPLED RECEPTORS

(Received for publication, November 27, 1996)

Shahla Verrall Dagger § , Maki Ishii § , Mian Chen Dagger § , Ling Wang Dagger § , Tracy Tram Dagger § and Shaun R. Coughlin Dagger §

From the Dagger  Cardiovascular Research Institute, the § Daiichi Research Center, and the  Department of Medicine, University of California, San Francisco, California 94143-0130

Thrombin activates human platelets and other cells in part by cleaving an unusual G protein-coupled receptor. Thrombin cleavage of this receptor's amino-terminal exodomain unmasks a new amino terminus. This then binds intramolecularly to the body of the receptor to trigger transmembrane signaling and activation of Gi- and Gq-like G proteins. Toward identifying the domains responsible for thrombin receptor-G protein interactions, we examined the signaling properties of chimeric receptors in which thrombin receptor cytoplasmic sequences replaced the cognate sequences in the Gs-coupled beta 2-adrenergic receptor (beta 2AR) or the Gi-coupled dopamine D2 receptor (D2R). In Xenopus oocytes, a chimeric beta 2AR bearing the thrombin receptor second cytoplasmic (C2) loop gained the ability to trigger intracellular Ca2+ release in response to adrenergic agonist, whereas a beta 2AR bearing the cognate C2 loop from the D2R did not. Similarly, in COS-7 cells, a chimeric D2R bearing the thrombin receptor C2 loop gained the ability to trigger phosphoinositide hydrolysis in response to dopaminergic agonist, apparently by coupling to a Gq-like G protein. No detectable Gs coupling was seen. Thus, the thrombin receptor C2 loop was able to confer Gq-like coupling in several different receptor contexts. These observations suggest that the thrombin receptor C2 loop specifies Gq coupling by directly contacting Gq or by contributing to a structure required for Gq coupling. The ability of the thrombin receptor C2 loop to function in the context of the D2R and beta 2AR strongly suggests that the transmembrane switching and G protein activation strategies used by the thrombin receptor must be very similar to those used by the D2R and beta 2AR despite the thrombin receptor's strikingly different liganding mechanism.


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