RGS2 is a component of the cellular stress response

Biochemical and Biophysical Research Communications

Volumn 426, Issue 1, 2012, Pages 129-134

  Nguyen, Chau H ^a   Zhao, Peishen ^a   Sobiesiak, Alina J ^a   Chidiac, Peter ^a  

^a UNIVERSITY OF WESTERN ONTARIO   (Canada)

Author keywords

Cellular stress response; Protein synthesis; RGS protein; Translation

Indexed keywords

PROTEOME; RGS2 PROTEIN; SMALL INTERFERING RNA;

ANIMAL CELL; ARTICLE; CELLULAR STRESS RESPONSE; CONTROLLED STUDY; EMBRYO; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN SYNTHESIS INHIBITION; REGULATORY MECHANISM; RNA INTERFERENCE; TEMPERATURE STRESS; UPREGULATION;

ANIMALS; APOPTOSIS; CELL LINE; EUKARYOTIC INITIATION FACTOR-2; FIBROBLASTS; GENE KNOCKDOWN TECHNIQUES; HEAT-SHOCK RESPONSE; MICE; PROTEIN BIOSYNTHESIS; PROTEOME; RGS PROTEINS; RNA, SMALL INTERFERING; STRESS, PHYSIOLOGICAL;

EID: 84866314953     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.08.050     Document Type: Article

References (34)

1. Proud C.G. EIF2 and the control of cell physiology. Semin. Cell. Dev. Biol. 2005, 16:3-12.
2. Holcik M., Sonenberg N. Translational control in stress and apoptosis. Nat. Rev. Mol. Cell Biol. 2005, 6:318-327.
3. Wek R.C., Jiang H.Y., Anthony T.G. Coping with stress: eIF2 kinases and translational control. Biochem. Soc. Trans. 2006, 34:7-11.
4. Kimball S.R. Eukaryotic initiation factor eIF2. Int. J. Biochem. Cell Biol. 1999, 31:25-29.
5. Spriggs K.A., Stoneley M., Bushell M., Willis A.E. Re-programming of translation following cell stress allows IRES-mediated translation to predominate. Biol. Cell 2008, 100:27-38.
6. Scheuner D., Song B., McEwen E., Liu C., Laybutt R., Gillespie P., Saunders T., Bonner-Weir S., Kaufman R.J. Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Nat. Rev. Mol. Cell Biol. 2001, 7:1165-1176.
7. McEwen E., Kedersha N., Song B., Scheuner D., Gilks N., Han A., Chen J.J., Anderson P., Kaufman R.J. Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure. J. Biol. Chem. 2005, 280:16925-16933.
8. Nguyen C.H., Ming H., Zhao P., Hugendubler L., Gros R., Kimball S.R., Chidiac P. Translational control by RGS2. J. Cell Biol. 2009, 186:755-765.
9. Ross E.M., Wilkie T.M. GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Annu. Rev. Biochem. 2000, 69:795-827.
10. Schoeber J.P., Topala C.N., Wang X., Diepens R.J., Lambers T.T., Hoenderop J.G., Bindels R.J. RGS2 inhibits the epithelial Ca2+ channel TRPV6. J. Biol. Chem. 2006, 281:29669-29674.
11. Heo K., Ha S.H., Chae Y.C., Lee S., Oh Y.S., Kim Y.H., Kim S.H., Kim J.H., Mizoguchi A., Itoh T.J., Kwon H.M., Ryu S.H., Suh P.G. RGS2 promotes formation of neurites by stimulating microtubule polymerization. Cell. Signal. 2006, 18:2182-2192.
12. Sethakorn N., Yau D.M., Dulin N.O. Non-canonical functions of RGS proteins. Cell Signal. 2010, 22:1274-1281.
13. de Araujo R.M., Oba Y., Moriyama K. Role of regulator of G-protein signaling 2 (RGS2) in periodontal ligament cells under mechanical stress. Cell Biochem. Funct. 2007, 25:753-758.
14. Siderovski D.P., Heximer S.P., Forsdyke D.R. A human gene encoding a putative basic helix-loop-helix phosphoprotein whose mRNA increases rapidly in cycloheximide-treated blood mononuclear cells. DNA Cell Biol. 1994, 13:125-147.
15. Song L., Jope R.S. Cellular stress increases RGS2 mRNA and decreases RGS4 mRNA levels in SH-SY5Y cells. Neurosci. Lett. 2006, 402:205-209.
16. Zmijewski J.W., Song L., Harkins L., Cobbs C.S., Jope R.S. Oxidative stress and heat shock stimulate RGS2 expression in 1321N1 astrocytoma cells. Arch. Biochem. Biophys. 2001, 392:192-196.
17. Hershey J.W. Translational control in mammalian cells. Annu. Rev. Biochem. 1991, 60:717-755.
18. Ma Y., Hendershot L.M. Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress. J. Biol. Chem. 2003, 278:34864-34873.
19. Novoa I., Zeng H., Harding H.P., Ron D. Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J. Cell Biol. 2001, 153:1011-1022.
20. Harding H.P., Zhang Y., Scheuner D., Chen J.J., Kaufman R.J., Ron D. Ppp 1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2alpha) dephosphorylation in mammalian development. Proc. Natl. Acad. Sci. USA 2009, 106:1832-1837.
21. Kojima E., Takeuchi A., Haneda M., Yagi A., Hasegawa T., Yamaki K., Takeda K., Akira S., Shimokata K., Isobe K. The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice. Faseb J. 2003, 17:1573-1575.
22. Heximer S.P., Cristillo A.D., Forsdyke D.R. Comparison of mRNA expression of two regulators of G-protein signaling, RGS1/BL34/1R20 and RGS2/G0S8, in cultured human blood mononuclear cells. DNA Cell Biol. 1997, 16:589-598.
23. Ingi T., Krumins A.M., Chidiac P., Brothers G.M., Chung S., Snow B.E., Barnes C.A., Lanahan A.A., Siderovski D.P., Ross E.M., Gilman A.G., Worley P.F. Dynamic regulation of RGS2 suggests a novel mechanism in G-protein signaling and neuronal plasticity. J. Neurosci. 1998, 18:7178-7188.
24. Clemens M.J. Translational regulation in cell stress and apoptosis. Roles of the eIF4E binding proteins. J. Cell. Mol. Med. 2001, 5:221-239.
25. Buchan J.R., Parker R. Eukaryotic stress granules: the ins and outs of translation. Nat. Rev. Mol. Cell Biol. 2009, 36:932-941.
26. Zhang K., Kaufman R.J. From endoplasmic-reticulum stress to the inflammatory response. Nature 2008, 454:455-462.
27. Vattem K.M., Wek R.C. Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells. Proc. Natl. Acad. Sci. USA 2004, 101:11269-11274.
28. Cheng Y.S., Lee T.S., Hsu H.C., Kou Y.R., Wu Y.L. Characterization of the transcriptional regulation of the regulator of G protein signaling 2 (RGS2) gene during 3T3-L1 preadipocyte differentiation. J. Cell. Biochem. 2008, 105:922-930.
29. McCaffrey R.L., Fawcett P., O'Riordan M., Lee K.D., Havell E.A., Brown P.O., Portnoy D.A. A specific gene expression program triggered by Gram-positive bacteria in the cytosol. Proc. Natl. Acad. Sci. USA 2004, 101:11386-11391.
30. Jennings J., Chen D., Feldman D. Transcriptional response of dermal fibroblasts in direct current electric fields. Bioelectromagnetics 2008, 29:394-405.
31. Endale M., Kim S.D., Lee W.M., Kim S., Suk K., Cho J.Y., Park H.J., Wagley Y., Kim S., Oh J.W., Rhee M.H. Ischemia induces regulator of G protein signaling 2 (RGS2) protein upregulation and enhances apoptosis in astrocytes. Am. J. Physiol. Cell Physiol. 2010, 298:C611-C623.
32. Kitamura C., Takahashi M., Kondoh Y., Tashiro H., Tashiro T. Identification of synaptic activity-dependent genes by exposure of cultured cortical neurons to tetrodotoxin followed by its withdrawal. J. Neurosci. Res. 2007, 85:2385-2399.
33. Roy A.A., Nunn C., Ming H., Zou M.X., Penninger J., Kirshenbaum L.A., Dixon S.J., Chidiac P. Up-regulation of endogenous RGS2 mediates cross-desensitization between Gs and Gq signaling in osteoblasts. J. Biol. Chem. 2006, 281:32684-32693.
34. Gu S., Anton A., Salim S., Blumer K.J., Dessauer C.W., Heximer S.P. Alternative translation initiation of human regulators of G-protein signaling-2 yields a set of functionally distinct proteins. Mol. Pharmacol. 2008, 73:1-11.