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The Journal of Neuroscience, 2000, 20:RC59:1-5

RAPID COMMUNICATION
Copurification of Brain G-Protein 5 with RGS6 and RGS7

Jian-Hua Zhang and William F. Simonds

Metabolic Diseases Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892

A structurally divergent G-protein  subunit expressed in brain and retina, G₅, exhibits functional specialization in its protein-protein interactions in vitro. In retina, G5 has been isolated in a soluble complex with regulator of G-protein signaling RGS7. The function and molecular associations of G₅ in brain are unknown. To identify tightly bound proteins associated with G₅ in the brain, it was immunoaffinity-purified from a nonionic detergent extract of washed mouse brain membranes using an antibody directed against its N terminus. Elution with cognate peptide revealed a broad band of 55 kDa that coeluted with G₅ on SDS-PAGE. The copurifying 55 kDa band was identified as a ~1:1 mixture of RGS6 and RGS7 by matrix-assisted laser desorption ionization mass spectroscopic analysis of tryptic peptides. G₅ and RGS7 could be reciprocally coimmunoprecipitated from unfractionated brain membrane extracts confirming the tight association of native proteins. In contrast, immunoblotting of the peptide eluate revealed no copurifying Gq/11, Gi1/2, G2, G3, or G7. These findings implicate RGS6 and RGS7 in the function of G₅ in the brain and suggest that a large fraction of membrane-targeted G₅ has no associated G subunit and therefore functions outside the canonical framework of G interactions.

Key words: signal transduction; G-proteins; regulators of G-protein signaling; Igs; affinity purification; mass spectroscopy

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Copyright © 2000 Society for Neuroscience  0270-6474/00/$05.00/0

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