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Gene Review

RGS7  -  regulator of G-protein signaling 7

Homo sapiens

Synonyms: Regulator of G-protein signaling 7
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Disease relevance of RGS7

  • Here we demonstrate that tumor necrosis factor (TNF)-alpha, an essential mediator of endotoxin-induced sepsis, prevents the proteasome-dependent degradation of RGS7, a regulator of G-protein signaling [1].
  • The subcellular localization of Gbeta(5) and RGS7 was examined in rat PC12 pheochromocytoma cells and mouse brain [2].
  • In situ hybridization revealed a transient, robust early increase in RGS7 mRNA levels in the dentate gyrus after ischemia [3].

High impact information on RGS7

  • Our findings indicate that TNF-mediated upregulation of RGS7 may contribute to sepsis-induced changes in central nervous function [1].
  • Upregulation of RGS7 may contribute to tumor necrosis factor-induced changes in central nervous function [1].
  • Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family [4].
  • Here, we identify R7BP, a novel neuronally expressed protein that binds R7-Gbeta5 complexes and shuttles them between the plasma membrane and nucleus [4].
  • Here we confirm through targeted mutagenesis of RGS7 that these ET-identified residues are critical for RGS domain regulation and are likely to function as global determinants of RGS function [5].

Biological context of RGS7

  • The inhibitory interaction between 14-3-3 and RGS7 requires phosphorylation of serine 434 of RGS7 [6].
  • RGS7 attenuates signal transduction through the G(alpha q) family of heterotrimeric G proteins in mammalian cells [7].
  • To gain insight into its function, we used yeast two-hybrid analysis to screen a human whole brain cDNA library in order to identify proteins that interact specifically with the N-terminus of human RGS7 (amino acid residues 1-248) [8].
  • Our results suggest that RGS7 could play a role in synaptic vesicle exocytosis through its interaction with snapin [8].
  • We observed that RGS4 mRNA and protein were concomitantly augmented with increased cell density and decreased by exposure of PC12M cells to nerve growth factor, whereas RGS7 was unaffected [9].

Anatomical context of RGS7

  • After expression in Sf9 cells, complexes of both RGS6 and RGS7 with the Gbeta5 subunit (but not Gbetas 1-4) are found in the cytosol [10].
  • Palmitoylation and plasma membrane targeting of RGS7 are promoted by alpha o [11].
  • Both nuclear and cytosolic localization of Gbeta(5) and RGS7 was evident in PC12 cells by immunocytochemical staining [2].
  • Endogenous levels of RGS7 exceeded RGS4 by 30-40-fold, and studies of cultured cells revealed regulatory differences between the two proteins [9].
  • Ischemia-induced increase in RGS7 mRNA expression in gerbil hippocampus [3].

Associations of RGS7 with chemical compounds

  • RGS7-deficient mice showed an increased response to both [D-Ala(2)]deltorphin II and DPDPE analgesic effects [12].
  • Cellular stimulation by TNF-alpha transiently decreased the phosphorylation of serine 434 of RGS7, abrogating the inhibitory interaction with 14-3-3 [6].
  • Binding of 14-3-3 is mediated by a conserved phosphoserine located in the Galpha-interacting portion of the RGS domain; interaction with 14-3-3 inhibits the GAP activity of RGS7, depends upon phosphorylation of a conserved residue within the RGS domain, and results in inhibition of GAP function [13].
  • To examine potential palmitoylation sites of RGS7, several cysteines were substituted with serines. beta(5)RGS7C133S failed to localize to plasma membranes when coexpressed with alpha(o), suggesting cysteine 133 of RGS7 as a putative palmitoylation site [11].
  • Coexpression of the proteins RGS3 and RGS7 together with CFTR and alphaG(i2) partially recovered activation by IBMX/forskolin [14].

Other interactions of RGS7

  • A single intracerebroventricular (i.c.v.) ED(80) analgesic dose of morphine gave rise to acute tolerance in control mice, but did not promote tolerance in RGS6, RGS7, RGS9-2, or RGS11 knockdown animals [12].
  • RGS7 and RGS17 had overlapping distribution profiles and were both noticeably enriched in the cerebellum [15].
  • The degradation of RGS7 is inhibited by interaction with a C-terminal domain of polycystin, the protein encoded by PKD1, a gene involved in autosomal-dominant polycystic kidney disease [16].
  • RGS4 N terminus fused to either full-length or the C terminus of RGS7 successfully complemented sst2Delta [17].
  • Here we show that 14-3-3 proteins associate with RGS7 and RGS3 [13].

Analytical, diagnostic and therapeutic context of RGS7

  • The reconstituted Gbeta5-RGS dimers are similar to the native retinal complex in their behavior on gel-filtration and cation-exchange chromatographies and can be immunoprecipitated with either anti-Gbeta5 or anti-RGS7 antibodies [18].


  1. Upregulation of RGS7 may contribute to tumor necrosis factor-induced changes in central nervous function. Benzing, T., Brandes, R., Sellin, L., Schermer, B., Lecker, S., Walz, G., Kim, E. Nat. Med. (1999) [Pubmed]
  2. Nuclear localization of G protein beta 5 and regulator of G protein signaling 7 in neurons and brain. Zhang, J.H., Barr, V.A., Mo, Y., Rojkova, A.M., Liu, S., Simonds, W.F. J. Biol. Chem. (2001) [Pubmed]
  3. Ischemia-induced increase in RGS7 mRNA expression in gerbil hippocampus. Shelat, P.B., Coulibaly, A.P., Wang, Q., Sun, A.Y., Sun, G.Y., Simonyi, A. Neurosci. Lett. (2006) [Pubmed]
  4. Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family. Drenan, R.M., Doupnik, C.A., Boyle, M.P., Muglia, L.J., Huettner, J.E., Linder, M.E., Blumer, K.J. J. Cell Biol. (2005) [Pubmed]
  5. Prediction and confirmation of a site critical for effector regulation of RGS domain activity. Sowa, M.E., He, W., Slep, K.C., Kercher, M.A., Lichtarge, O., Wensel, T.G. Nat. Struct. Biol. (2001) [Pubmed]
  6. Interaction of 14-3-3 protein with regulator of G protein signaling 7 is dynamically regulated by tumor necrosis factor-alpha. Benzing, T., Köttgen, M., Johnson, M., Schermer, B., Zentgraf, H., Walz, G., Kim, E. J. Biol. Chem. (2002) [Pubmed]
  7. RGS7 attenuates signal transduction through the G(alpha q) family of heterotrimeric G proteins in mammalian cells. Shuey, D.J., Betty, M., Jones, P.G., Khawaja, X.Z., Cockett, M.I. J. Neurochem. (1998) [Pubmed]
  8. Snapin interacts with the N-terminus of regulator of G protein signaling 7. Hunt, R.A., Edris, W., Chanda, P.K., Nieuwenhuijsen, B., Young, K.H. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  9. Differentially regulated expression of endogenous RGS4 and RGS7. Krumins, A.M., Barker, S.A., Huang, C., Sunahara, R.K., Yu, K., Wilkie, T.M., Gold, S.J., Mumby, S.M. J. Biol. Chem. (2004) [Pubmed]
  10. Regulators of G protein signaling 6 and 7. Purification of complexes with gbeta5 and assessment of their effects on g protein-mediated signaling pathways. Posner, B.A., Gilman, A.G., Harris, B.A. J. Biol. Chem. (1999) [Pubmed]
  11. Palmitoylation and plasma membrane targeting of RGS7 are promoted by alpha o. Takida, S., Fischer, C.C., Wedegaertner, P.B. Mol. Pharmacol. (2005) [Pubmed]
  12. The R7 subfamily of RGS proteins assists tachyphylaxis and acute tolerance at mu-opioid receptors. Garzón, J., López-Fando, A., Sánchez-Blázquez, P. Neuropsychopharmacology (2003) [Pubmed]
  13. 14-3-3 interacts with regulator of G protein signaling proteins and modulates their activity. Benzing, T., Yaffe, M.B., Arnould, T., Sellin, L., Schermer, B., Schilling, B., Schreiber, R., Kunzelmann, K., Leparc, G.G., Kim, E., Walz, G. J. Biol. Chem. (2000) [Pubmed]
  14. Control of the cystic fibrosis transmembrane conductance regulator by alphaG(i) and RGS proteins. Schreiber, R., Kindle, P., Benzing, T., Walz, G., Kunzelmann, K. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  15. Selective expression of regulators of G-protein signaling (RGS) in the human central nervous system. Larminie, C., Murdock, P., Walhin, J.P., Duckworth, M., Blumer, K.J., Scheideler, M.A., Garnier, M. Brain Res. Mol. Brain Res. (2004) [Pubmed]
  16. Interaction between RGS7 and polycystin. Kim, E., Arnould, T., Sellin, L., Benzing, T., Comella, N., Kocher, O., Tsiokas, L., Sukhatme, V.P., Walz, G. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  17. Analysis of chimeric RGS proteins in yeast for the functional evaluation of protein domains and their potential use in drug target validation. Ajit, S.K., Young, K.H. Cell. Signal. (2005) [Pubmed]
  18. Gbeta5 prevents the RGS7-Galphao interaction through binding to a distinct Ggamma-like domain found in RGS7 and other RGS proteins. Levay, K., Cabrera, J.L., Satpaev, D.K., Slepak, V.Z. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
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