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Originally published In Press as doi:10.1074/jbc.M009247200 on January 4, 2001

J. Biol. Chem., Vol. 276, Issue 13, 10284-10289, March 30, 2001
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Nuclear Localization of G Protein beta 5 and Regulator of G Protein Signaling 7 in Neurons and Brain*

Jian-Hua Zhang, Valarie A. BarrDagger §, Yinyuan Mo, Alexandra M. Rojkova, Shaohua Liu||, and William F. Simonds**

From the Metabolic Diseases Branch and the Dagger  Diabetes Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, and the  Department of Molecular Genetics, University of Illinois at Chicago, College of Medicine, Chicago, Illinois 60607

The role that Gbeta 5 regulator of G protein signaling (RGS) complexes play in signal transduction in brain remains unknown. The subcellular localization of Gbeta 5 and RGS7 was examined in rat PC12 pheochromocytoma cells and mouse brain. Both nuclear and cytosolic localization of Gbeta 5 and RGS7 was evident in PC12 cells by immunocytochemical staining. Subcellular fractionation of PC12 cells demonstrated Gbeta 5 immunoreactivity in the membrane, cytosolic, and nuclear fractions. Analysis by limited proteolysis confirmed the identity of Gbeta 5 in the nuclear fraction. Subcellular fractionation of mouse brain demonstrated Gbeta 5 and RGS7 but not Ggamma 2/3 immunoreactivity in the nuclear fraction. RGS7 and Gbeta 5 were tightly complexed in the brain nuclear extract as evidenced by their coimmunoprecipitation with anti-RGS7 antibodies. Chimeric protein constructs containing green fluorescent protein fused to wild-type Gbeta 5 but not green fluorescent fusion proteins with Gbeta 1 or a mutant Gbeta 5 impaired in its ability to bind to RGS7 demonstrated nuclear localization in transfected PC12 cells. These findings suggest that Gbeta 5 undergoes nuclear translocation in neurons via an RGS-dependent mechanism. The novel intracellular distribution of Gbeta 5·RGS protein complexes suggests a potential role in neurons communicating between classical heterotrimeric G protein subunits and/or their effectors at the plasma membrane and the cell nucleus.

* 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.

§ Present address: Clinical Endocrinology Branch, NIDDK, National Institutes of Health, Bethesda, MD 20892.

|| Present address: Dept. of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, NY 11794.

** To whom correspondence should be addressed: Metabolic Diseases Branch, NIDDK, National Institutes of Health, Bldg. 10, Rm. 8C-101, 10 Center Dr., MSC 1752, Bethesda, MD 20892-1752. Tel.: 301-496-9299; Fax: 301-402-0374, E-mail: wfs@helix.nih.gov.

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