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RGS3  -  regulator of G-protein signaling 3

Homo sapiens

Synonyms: C2PA, FLJ20370, PDZ-RGS3, RGP3, Regulator of G-protein signaling 3
 
 
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Disease relevance of RGS3

  • U373MG glioma cell clones overexpressing RGS3 or RGS4 showed an increase of both adhesion and migration [1].
  • RGS3 and RGS4 gene expression was markedly enhanced in two model systems of cardiac hypertrophy: growth factor-stimulated cultured neonatal rat cardiomyocytes and pulmonary artery-banded (PAB) mice [2].
  • This article provides detailed information on the use and power of retrovirus-mediated overexpression of RGS proteins in dorsal root ganglion neurons to isolate and identify the mechanisms underlying the initiation of RGS3-dependent inhibitory activity [3].
  • In contrast, the distribution of PDZ-RGS3 does not change during heat stress [4].
 

High impact information on RGS3

  • In dorsal root ganglion neurons overexpressing RGS3, we find that G protein signaling is rapidly terminated (or "desensitized") by calcium influx through voltage-gated channels [5].
  • A naturally occurring variant of RGS3 that lacks the EF hand neither binds calcium nor produces rapid desensitization, giving rise instead to a slower calcium-dependent desensitization that is attenuated by a calmodulin antagonist [5].
  • RGS3 mediates a calcium-dependent termination of G protein signaling in sensory neurons [5].
  • In complex neural circuits subjected to abundant synaptic inhibition by G proteins (as occurs in dorsal spinal cord), rapid termination of inhibition by electrical activity by EF hand-containing RGS3 may ensure the faithful transmission of information from the most active sensory inputs [5].
  • These data indicate that RGS3 inhibits G protein-coupled receptor signaling by a complex mechanism involving its translocation to the membrane in addition to its established function as a GTPase-activating protein [6].
 

Biological context of RGS3

 

Anatomical context of RGS3

 

Associations of RGS3 with chemical compounds

  • Regulator of G-protein signaling 3 (RGS3) inhibits Gbeta1gamma 2-induced inositol phosphate production, mitogen-activated protein kinase activation, and Akt activation [10].
  • The effect of endothelin-1 was also mimicked by calcium ionophore A23187, suggesting the importance of Ca2+ in the mechanism of redistribution of RGS3 [6].
  • Palmitic acid incorporation into RGS3 was dependent on agonist occupancy of GnRHR, whereas palmitoylation of RGS10 was constitutive [13].
  • C2PA is a novel protein that contains a C2 membrane binding domain, a PDZ protein/protein interaction domain, and an ATP/GTP binding domain [14].
 

Physical interactions of RGS3

 

Regulatory relationships of RGS3

 

Other interactions of RGS3

  • RGS3 and RGS3CT had G(qalpha) GAP activity similar to that of RGS4 [11].
  • Regulator of G-protein signaling 3 (RGS3) enhances the intrinsic rate at which Galpha(i) and Galpha(q) hydrolyze GTP to GDP, thereby limiting the duration in which GTP-Galpha(i) and GTP-Galpha(q) can activate effectors [10].
  • Thus, RGS3 may limit Gbetagamma signaling not only by virtue of its GTPase-activating protein activity for Galpha subunits, but also by directly interfering with the activation of effectors [10].
  • Consistent with the in vivo results, RGS3 inhibits Gbetagamma-mediated activation of phospholipase Cbeta in vitro [10].
  • Thus, RGS3 can impair Gi- (but not Gz-) and Gq-mediated signaling in hematopoietic and other cell types by acting as a GAP for G(ialpha) and G(qalpha) subfamily members and as a potent G(qalpha) subfamily effector antagonist [11].
 

Analytical, diagnostic and therapeutic context of RGS3

  • Using long-distance PCR, we amplified and characterized the entire coding and 5'-untranslated region of the human RGS3 gene [8].
  • RT-PCR analysis demonstrated that this Medaka RGS3-like protein (MeRGS3L) is mainly expressed in skin and heart [16].
  • Confocal microscopy was used to examine the intracellular locations of four RGS3-enhanced green fluorescent protein fusion proteins [17].

References

  1. Regulators of G-protein signaling 3 and 4 (RGS3, RGS4) are associated with glioma cell motility. Tatenhorst, L., Senner, V., Püttmann, S., Paulus, W. J. Neuropathol. Exp. Neurol. (2004) [Pubmed]
  2. RGS3 and RGS4 are GTPase activating proteins in the heart. Zhang, S., Watson, N., Zahner, J., Rottman, J.N., Blumer, K.J., Muslin, A.J. J. Mol. Cell. Cardiol. (1998) [Pubmed]
  3. Assays of RGS3 activation and modulation. Tosetti, P., Dunlap, K. Meth. Enzymol. (2004) [Pubmed]
  4. C2PA is a nuclear protein implicated in the heat shock response. Hirabayashi, S., Ohno, H., Iida, J., Hata, Y. J. Cell. Biochem. (2002) [Pubmed]
  5. RGS3 mediates a calcium-dependent termination of G protein signaling in sensory neurons. Tosetti, P., Pathak, N., Jacob, M.H., Dunlap, K. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  6. RGS3 inhibits G protein-mediated signaling via translocation to the membrane and binding to Galpha11. Dulin, N.O., Sorokin, A., Reed, E., Elliott, S., Kehrl, J.H., Dunn, M.J. Mol. Cell. Biol. (1999) [Pubmed]
  7. RGS3 interacts with 14-3-3 via the N-terminal region distinct from the RGS (regulator of G-protein signalling) domain. Niu, J., Scheschonka, A., Druey, K.M., Davis, A., Reed, E., Kolenko, V., Bodnar, R., Voyno-Yasenetskaya, T., Du, X., Kehrl, J., Dulin, N.O. Biochem. J. (2002) [Pubmed]
  8. Genomic organization, 5'-flanking region, and chromosomal localization of the human RGS3 gene. Chatterjee, T.K., Eapen, A., Kanis, A.B., Fisher, R.A. Genomics (1997) [Pubmed]
  9. Evidence for a short form of RGS3 preferentially expressed in the human heart. Mittmann, C., Schüler, C., Chung, C.H., Höppner, G., Nose, M., Kehrl, J.H., Wieland, T. Naunyn Schmiedebergs Arch. Pharmacol. (2001) [Pubmed]
  10. Regulator of G-protein signaling 3 (RGS3) inhibits Gbeta1gamma 2-induced inositol phosphate production, mitogen-activated protein kinase activation, and Akt activation. Shi, C.S., Lee, S.B., Sinnarajah, S., Dessauer, C.W., Rhee, S.G., Kehrl, J.H. J. Biol. Chem. (2001) [Pubmed]
  11. RGS3 is a GTPase-activating protein for g(ialpha) and g(qalpha) and a potent inhibitor of signaling by GTPase-deficient forms of g(qalpha) and g(11alpha). Scheschonka, A., Dessauer, C.W., Sinnarajah, S., Chidiac, P., Shi, C.S., Kehrl, J.H. Mol. Pharmacol. (2000) [Pubmed]
  12. Regulation of chemotactic and proadhesive responses to chemoattractant receptors by RGS (regulator of G-protein signaling) family members. Bowman, E.P., Campbell, J.J., Druey, K.M., Scheschonka, A., Kehrl, J.H., Butcher, E.C. J. Biol. Chem. (1998) [Pubmed]
  13. Regulation of RGS3 and RGS10 palmitoylation by GnRH. Castro-Fernández, C., Janovick, J.A., Brothers, S.P., Fisher, R.A., Ji, T.H., Conn, P.M. Endocrinology (2002) [Pubmed]
  14. C2PA, a new protein expressed during mouse spermatogenesis. Linares, J.L., Wendling, C., Tomasetto, C., Rio, M.C. FEBS Lett. (2000) [Pubmed]
  15. A regulator of G-protein signaling in olfactory receptor neurons. Bruch, R.C., Medler, K.F. Neuroreport (1996) [Pubmed]
  16. Molecular cloning and characterization of a new RGS protein of Medaka. Itoh, M., Nagatomo, K., Kubo, Y., Sugimoto, M., Saitoh, O. Gene (2005) [Pubmed]
  17. Muscarinic modulation of Cav2.3 (R-type) calcium channels is antagonized by RGS3 and RGS3T. Toro-Castillo, C., Thapliyal, A., Gonzalez-Ochoa, H., Adams, B.A., Meza, U. Am. J. Physiol., Cell Physiol. (2007) [Pubmed]
 
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