RGS10
Regulator of G-protein signaling 10 is a protein that in humans is encoded by the RGS10 gene.[1][2]
Regulator of G protein signaling (RGS) family members are regulatory molecules that act as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins are able to deactivate G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. Regulator of G protein signaling 10 belongs to this family. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. This protein associates specifically with the activated forms of the two related G-protein subunits, G-alphai3 and G-alphaz but fails to interact with the structurally and functionally distinct G-alpha subunits. Regulator of G protein signaling 10 protein is localized in the nucleus. Two transcript variants encoding different isoforms have been found for this gene.[2]
Interactions
RGS10 has been shown to interact with SAP18[3] and GNAI3.[1]
References
- ^ a b Hunt TW, Fields TA, Casey PJ, Peralta EG (Oct 1996). "RGS10 is a selective activator of G alpha i GTPase activity". Nature 383 (6596): 175–7. doi:10.1038/383175a0. PMID 8774883.
- ^ a b "Entrez Gene: RGS10 regulator of G-protein signalling 10". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6001.
- ^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.
Further reading
- Popov S, Yu K, Kozasa T, Wilkie TM (1997). "The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro.". Proc. Natl. Acad. Sci. U.S.A. 94 (14): 7216–20. doi:10.1073/pnas.94.14.7216. PMC 23796. PMID 9207071. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=23796.
- Tu Y, Wang J, Ross EM (1997). "Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G protein alpha subunits.". Science 278 (5340): 1132–5. doi:10.1126/science.278.5340.1132. PMID 9353196.
- Tu Y, Popov S, Slaughter C, Ross EM (2000). "Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10.". J. Biol. Chem. 274 (53): 38260–7. doi:10.1074/jbc.274.53.38260. PMID 10608901.
- Popov SG, Krishna UM, Falck JR, Wilkie TM (2000). "Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity.". J. Biol. Chem. 275 (25): 18962–8. doi:10.1074/jbc.M001128200. PMID 10747990.
- Chatterjee TK, Fisher RA (2000). "Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs.". J. Biol. Chem. 275 (31): 24013–21. doi:10.1074/jbc.M002082200. PMID 10791963.
- Burgon PG, Lee WL, Nixon AB, et al. (2001). "Phosphorylation and nuclear translocation of a regulator of G protein signaling (RGS10).". J. Biol. Chem. 276 (35): 32828–34. doi:10.1074/jbc.M100960200. PMID 11443111.
- Gagnon AW, Murray DL, Leadley RJ (2002). "Cloning and characterization of a novel regulator of G protein signalling in human platelets.". Cell. Signal. 14 (7): 595–606. doi:10.1016/S0898-6568(02)00012-8. PMID 11955952.
- Castro-Fernández C, Conn PM (2003). "Regulation of the gonadotropin-releasing hormone receptor (GnRHR) by RGS proteins: role of the GnRHR carboxyl-terminus.". Mol. Cell. Endocrinol. 191 (2): 149–56. doi:10.1016/S0303-7207(02)00082-5. PMID 12062898.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Oh JH, Yang JO, Hahn Y, et al. (2006). "Transcriptome analysis of human gastric cancer.". Mamm. Genome 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674.
- Lee HK, Rhee KH, Kim CW, et al. (2006). "Crystallization and preliminary X-ray crystallographic analysis of human RGS10 complexed with Galphai3.". Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (Pt 9): 831–3. doi:10.1107/S1744309105023602. PMC 1978115. PMID 16511171. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1978115.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.
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PDB gallery
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2dlr: Solution structure of the RGS domain of human Regulator of G-protein signaling 10
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2i59: Solution structure of RGS10
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2ihb: Crystal structure of the heterodimeric complex of human RGS10 and activated Gi alpha 3
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