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Rgs2  -  regulator of G-protein signaling 2

Mus musculus

Synonyms: GOS8, RGS2, Regulator of G-protein signaling 2
 
 
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Disease relevance of Rgs2

  • 5. Bordetella pertussis toxin completely abolished ACh-mediated current amplification of GIRK channels coexpressed with or without RGS2 [1].
  • By diminishing cGK activity, endothelial dysfunction may impair RGS2 activation, thereby blunting vascular relaxation and contributing to hypertension [2].
 

Psychiatry related information on Rgs2

 

High impact information on Rgs2

  • We also show that this locus can be subdivided into three regions, one of which contains Rgs2, which encodes a regulator of G protein signaling [4].
  • Genetic dissection of a behavioral quantitative trait locus shows that Rgs2 modulates anxiety in mice [4].
  • Rgs2-/- mice develop marked hypertension, and their blood vessels show enhanced contraction and decreased cGMP-mediated relaxation [5].
  • Our study shows that RGS-2 is required for normal vascular function and blood pressure and is a new drug development target for hypertension [5].
  • When expressed in Xenopus laevis oocytes, SPL markedly increased inhibition of alpha-adrenergic receptor (alphaAR) Ca2+ signalling by RGS2 [6].
 

Biological context of Rgs2

  • Within the pituitary, Rgs2 was expressed in undifferentiated cells, and was downregulated at the completion of the hormone cell differentiation [7].
  • CD40 signaling, by contrast, fails to cause rapid up-regulation of RGS1 or RGS2 [8].
  • Both rgs2+/- and rgs2-/- mice exhibited a strong hypertensive phenotype, renovascular abnormalities, persistent constriction of the resistance vasculature, and prolonged response of the vasculature to vasoconstrictors in vivo [9].
  • Analysis of P2Y receptor-mediated Ca2+ signaling in vascular smooth muscle cells in vitro indicated that loss of RGS2 increased agonist potency and efficacy and slowed the kinetics of signal termination [9].
  • RGS2, a GTPase-activating protein for Gqalpha that is critical for blood pressure homeostasis, has been suggested to serve as an effector of the NO-cGMP pathway that promotes vascular relaxation based on studies of aortic rings in vitro [10].
 

Anatomical context of Rgs2

  • One gene that was up-regulated at later stages of chondrocyte differentiation was Rgs2 [11].
  • Overexpression of Rgs2 in the chondrogenic cell line ATDC5 resulted in accelerated hypertrophic differentiation, thus providing functional validation of microarray data [11].
  • Regulation of T cell activation, anxiety, and male aggression by RGS2 [12].
  • We inhibited endogenous Galphaq function by single cell microinjection of anti-Galphaq/11 antibody or RGS2 protein (a GAP protein for Galphaq), followed by immunostaining to assess GLUT4 translocation in 3T3-L1 adipocytes [13].
  • The result of these adaptive mechanisms was the reduced excitability of Ca(2+) signaling, as reflected by the markedly reduced response of RGS2(-/-) cells to changes in the endoplasmic reticulum Ca(2+) load and to an increase in extracellular Ca(2+) [14].
 

Associations of Rgs2 with chemical compounds

 

Regulatory relationships of Rgs2

 

Other interactions of Rgs2

  • Furthermore, overexpression of the osteoblast-specific transcription factor Runx2 also led to a stimulation of RGS-2 promoter activity [18].
  • RGS2: a "turn-off" in hypertension [19].
 

Analytical, diagnostic and therapeutic context of Rgs2

References

  1. New roles for RGS2, 5 and 8 on the ratio-dependent modulation of recombinant GIRK channels expressed in Xenopus oocytes. Herlitze, S., Ruppersberg, J.P., Mark, M.D. J. Physiol. (Lond.) (1999) [Pubmed]
  2. Regulation of RGS2 and second messenger signaling in vascular smooth muscle cells by cGMP-dependent protein kinase. Osei-Owusu, P., Sun, X., Drenan, R.M., Steinberg, T.H., Blumer, K.J. J. Biol. Chem. (2007) [Pubmed]
  3. Rgs4 mRNA expression is decreased in the brain of Fmr1 knockout mouse. Tervonen, T., Akerman, K., Oostra, B.A., Castrén, M. Brain Res. Mol. Brain Res. (2005) [Pubmed]
  4. Genetic dissection of a behavioral quantitative trait locus shows that Rgs2 modulates anxiety in mice. Yalcin, B., Willis-Owen, S.A., Fullerton, J., Meesaq, A., Deacon, R.M., Rawlins, J.N., Copley, R.R., Morris, A.P., Flint, J., Mott, R. Nat. Genet. (2004) [Pubmed]
  5. Regulator of G-protein signaling-2 mediates vascular smooth muscle relaxation and blood pressure. Tang, K.M., Wang, G.R., Lu, P., Karas, R.H., Aronovitz, M., Heximer, S.P., Kaltenbronn, K.M., Blumer, K.J., Siderovski, D.P., Zhu, Y., Mendelsohn, M.E., Tang, M., Wang, G. Nat. Med. (2003) [Pubmed]
  6. Spinophilin regulates Ca2+ signalling by binding the N-terminal domain of RGS2 and the third intracellular loop of G-protein-coupled receptors. Wang, X., Zeng, W., Soyombo, A.A., Tang, W., Ross, E.M., Barnes, A.P., Milgram, S.L., Penninger, J.M., Allen, P.B., Greengard, P., Muallem, S. Nat. Cell Biol. (2005) [Pubmed]
  7. Developmentally regulated expression of the regulator of G-protein signaling gene 2 (Rgs2) in the embryonic mouse pituitary. Wilson, L.D., Ross, S.A., Lepore, D.A., Wada, T., Penninger, J.M., Thomas, P.Q. Gene Expr. Patterns (2005) [Pubmed]
  8. RGS molecule expression in murine B lymphocytes and ability to down-regulate chemotaxis to lymphoid chemokines. Reif, K., Cyster, J.G. J. Immunol. (2000) [Pubmed]
  9. Hypertension and prolonged vasoconstrictor signaling in RGS2-deficient mice. Heximer, S.P., Knutsen, R.H., Sun, X., Kaltenbronn, K.M., Rhee, M.H., Peng, N., Oliveira-dos-Santos, A., Penninger, J.M., Muslin, A.J., Steinberg, T.H., Wyss, J.M., Mecham, R.P., Blumer, K.J. J. Clin. Invest. (2003) [Pubmed]
  10. RGS2 is a mediator of nitric oxide action on blood pressure and vasoconstrictor signaling. Sun, X., Kaltenbronn, K.M., Steinberg, T.H., Blumer, K.J. Mol. Pharmacol. (2005) [Pubmed]
  11. Microarray analyses of gene expression during chondrocyte differentiation identifies novel regulators of hypertrophy. James, C.G., Appleton, C.T., Ulici, V., Underhill, T.M., Beier, F. Mol. Biol. Cell (2005) [Pubmed]
  12. Regulation of T cell activation, anxiety, and male aggression by RGS2. Oliveira-Dos-Santos, A.J., Matsumoto, G., Snow, B.E., Bai, D., Houston, F.P., Whishaw, I.Q., Mariathasan, S., Sasaki, T., Wakeham, A., Ohashi, P.S., Roder, J.C., Barnes, C.A., Siderovski, D.P., Penninger, J.M. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  13. G alpha-q/11 protein plays a key role in insulin-induced glucose transport in 3T3-L1 adipocytes. Imamura, T., Vollenweider, P., Egawa, K., Clodi, M., Ishibashi, K., Nakashima, N., Ugi, S., Adams, J.W., Brown, J.H., Olefsky, J.M. Mol. Cell. Biol. (1999) [Pubmed]
  14. Role of regulator of G protein signaling 2 (RGS2) in Ca(2+) oscillations and adaptation of Ca(2+) signaling to reduce excitability of RGS2-/- cells. Wang, X., Huang, G., Luo, X., Penninger, J.M., Muallem, S. J. Biol. Chem. (2004) [Pubmed]
  15. RGS proteins determine signaling specificity of Gq-coupled receptors. Xu, X., Zeng, W., Popov, S., Berman, D.M., Davignon, I., Yu, K., Yowe, D., Offermanns, S., Muallem, S., Wilkie, T.M. J. Biol. Chem. (1999) [Pubmed]
  16. Reduced expression of regulator of G-protein signaling 2 (RGS2) in hypertensive patients increases calcium mobilization and ERK1/2 phosphorylation induced by angiotensin II. Semplicini, A., Lenzini, L., Sartori, M., Papparella, I., Calò, L.A., Pagnin, E., Strapazzon, G., Benna, C., Costa, R., Avogaro, A., Ceolotto, G., Pessina, A.C. J. Hypertens. (2006) [Pubmed]
  17. Parathyroid hormone induces RGS-2 expression by a cyclic adenosine 3',5'-monophosphate-mediated pathway in primary neonatal murine osteoblasts. Tsingotjidou, A., Nervina, J.M., Pham, L., Bezouglaia, O., Tetradis, S. Bone (2002) [Pubmed]
  18. Analysis of regulator of G-protein signaling-2 (RGS-2) expression and function in osteoblastic cells. Thirunavukkarasu, K., Halladay, D.L., Miles, R.R., Geringer, C.D., Onyia, J.E. J. Cell. Biochem. (2002) [Pubmed]
  19. RGS2: a "turn-off" in hypertension. Le, T.H., Coffman, T.M. J. Clin. Invest. (2003) [Pubmed]
  20. Expression of regulator of G-protein signaling protein-2 gene in the rat ovary at the time of ovulation. Ujioka, T., Russell, D.L., Okamura, H., Richards, J.S., Espey, L.L. Biol. Reprod. (2000) [Pubmed]
 
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