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Originally published In Press as doi:10.1074/jbc.M001535200 on June 5, 2000

J. Biol. Chem., Vol. 275, Issue 32, 24872-24880, August 11, 2000
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Complexes of the G Protein Subunit Gbeta 5 with the Regulators of G Protein Signaling RGS7 and RGS9
CHARACTERIZATION IN NATIVE TISSUES AND IN TRANSFECTED CELLS*

D. Scott WitherowDagger , Qiang WangDagger , Konstatin LevayDagger , Jorge L. CabreraDagger , Jeannie Chen§, Gary B. Willars, and Vladlen Z. SlepakDagger ||

From the Dagger  Department of Molecular and Cellular Pharmacology and the Neuroscience Program, University of Miami School of Medicine, Miami, Florida 33136, the § Department of Ophthalmology, University of Southern California School of Medicine, Los Angeles, California 90033, and the  Department of Cell Physiology and Pharmacology, University of Leicester, Leicester LE1 9HN, United Kingdom

A novel protein class, termed regulators of G protein signaling (RGS), negatively regulates G protein pathways through a direct interaction with Galpha subunits and stimulation of GTP hydrolysis. An RGS subfamily including RGS6, -7, -9, and -11, which contain a characteristic Ggamma -like domain, also has the unique ability to interact with the G protein beta  subunit Gbeta 5. Here, we examined the behavior of Gbeta 5, RGS7, RGS9, and Galpha in tissue extracts using immunoprecipitation and conventional chromatography. Native Gbeta 5 and RGS7 from brain, as well as photoreceptor-specific Gbeta 5L and RGS9, always co-purified as tightly associated dimers, and neither RGS-free Gbeta 5 nor Gbeta 5-free RGS could be detected. Co-expression in COS-7 cells of Gbeta 5 dramatically increased the protein level of RGS7 and vice versa, indicating that cells maintain Gbeta 5:RGS stoichiometry in a manner similar to Gbeta gamma complexes. This mechanism is non-transcriptional and is based on increased protein stability upon dimerization. Thus, analysis of native Gbeta 5-RGS and their coupled expression argue that in vivo, Gbeta 5 and Ggamma -like domain-containing RGSs only exist as heterodimers. Native Gbeta 5-RGS7 did not co-precipitate or co-purify with Galpha o or Galpha q; nor did Gbeta 5L-RGS9 with Galpha t. However, in transfected cells, RGS7 and Gbeta 5-RGS7 inhibited Galpha q-mediated Ca2+ response to muscarinic M3 receptor activation. Thus, Gbeta 5-RGS dimers differ from other RGS proteins in that they do not bind to Galpha with high affinity, but they can still inhibit G protein signaling.

* This work was supported by a predoctoral fellowship from the American Heart Association, Florida/Puerto Rico Affiliate (to D. S. W.); by a Young Investigator award from the National Alliance for Research on Schizophrenia and Depression (to K. L.); by a predoctoral fellowship from the American Heart Association, Florida/Puerto Rico Affiliate (to J. L. C.); by National Institutes of Health RO1 Grants EY12155 and EY12703, Research to Prevent Blindness, and the Ruth and Milton Steinbach Fund (to J. C.); and by National Institutes of Health RO1 grants GM60019 and EY 12982, Pharmaceutical Research and Manufacturers of America Foundation, and Fight for Sight Research to Prevent Blindness America Foundation (to V. Z. S.).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: University of Miami School of Medicine R-189, 1600 N.W. 10th Ave., Miami, FL 33136. Tel.: 305-243-3430; Fax: 305-243-4555; E-mail: vslepak@newssun.med. miami.edu.

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