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Journal of Pharmacology And Experimental Therapeutics Fast Forward
First published on February 11, 2003; DOI: 10.1124/jpet.102.048637

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Vol. 305, Issue 2, 460-466, May 2003

Direct Interactions between the Heterotrimeric G Protein Subunit Gbeta 5 and the G Protein gamma  Subunit-Like Domain-Containing Regulator of G Protein Signaling 11: Gain of Function of Cyan Fluorescent Protein-Tagged Ggamma 3

Janice Y. Zhou, Peter T. Toth and Richard J. Miller

Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Chicago, Illinois

We used fluorescence resonance energy transfer imaging of enhanced cyan fluorescent protein (CFP)-tagged and enhanced yellow fluorescent protein (YFP)-tagged protein pairs to examine the hypothesis that G protein gamma  subunit-like (GGL) domain-containing regulators of G protein signaling (RGS) can directly bind to the Gbeta 5 subunit of heterotrimeric G proteins in vivo. We observed that Gbeta 5 could interact with Ggamma 2 and Ggamma 13, after their expression in human embryonic kidney 293 cells. Interestingly, although untagged Ggamma 3 did not interact with Gbeta 5, CFP-tagged Ggamma 3 strongly interacted with YFP-tagged Gbeta 5 in FRET studies. Moreover, CFP-Ggamma 3 supported Ca2+ channel inhibition when paired with Gbeta 5 or YFP-Gbeta 5, indicating a "gain of function" for CFP-Ggamma 3. Gbeta 5 could also interact with RGS11 and its N-terminal, but not its C-terminal domain. On the other hand, RGS11 did not interact with Gbeta 1. These studies demonstrate that the GGL domain-containing N terminus of RGS 11 can directly interact with Gbeta 5 in vivo and supports the hypothesis that this interaction may contribute to the specificity of Gbeta 5 interactions with cellular effector molecules.

0022-3565/03/3052-0460$07.00/0
THE JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS
Copyright © 2003 by The American Society for Pharmacology and Experimental Therapeutics


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