Redox regulation of Ran GTPase

Biochemical and Biophysical Research Communications

Volumn 376, Issue 3, 2008, Pages 568-572

  Heo, Jongyun ^a  

^a UNIVERSITY OF TEXAS AT ARLINGTON   (United States)

Author keywords

Cell cycle; Nuclear import; Oxidative stress; Ran; Reactive nitrogen species; Redox agent

Indexed keywords

CYSTEINE; GUANOSINE TRIPHOSPHATASE; NITROGEN DIOXIDE; PHENYLALANINE; RAN PROTEIN; REACTIVE NITROGEN SPECIES;

ARTICLE; CELL CYCLE; DISSOCIATION; ELECTROSPRAY MASS SPECTROMETRY; ENZYME KINETICS; NUCLEAR IMPORT; OXIDATIVE STRESS; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION;

CYSTEINE; GUANOSINE TRIPHOSPHATE; NITROGEN DIOXIDE; OXIDATION-REDUCTION; OXIDATIVE STRESS; RAN GTP-BINDING PROTEIN;

EID: 53149120984     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.09.016     Document Type: Article

References (40)

1. Dasso M. The Ran GTPase: theme and variations. Curr. Biol. 12 (2002) R502-R508
2. Cook A., Bono F., Jinek M., and Conti E. Structural biology of nucleocytoplasmic transport. Annu. Rev. Biochem. 76 (2007) 647-671
3. Geyer M., and Wittinghofer A. GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins. Curr. Opin. Struct. Biol. 7 (1997) 786-792
4. Renault L., Kuhlmann J., Henkel A., and Wittinghofer A. Structural basis for guanine nucleotide exchange on Ran by the regulator of chromosome condensation (RCC1). Cell 105 (2001) 245-255
5. Knight J.A. Review: free radicals, antioxidants, and the immune system. Ann. Clin. Lab. Sci. 30 (2000) 145-158
6. Ozben T. Oxidative stress and apoptosis: impact on cancer therapy. J. Pharm. Sci. 96 (2007) 2181-2196
7. Augusto O., Bonini M.G., Amanso A.M., Linares E., Santos C.C., and De Menezes S.L. Nitrogen dioxide and carbonate radical anion: two emerging radicals in biology. Free Radic. Biol. Med. 32 (2002) 841-859
8. Forstermann U., and Kleinert H. Nitric oxide synthase: expression and expressional control of the three isoforms. Naunyn Schmiedebergs Arch. Pharmacol. 352 (1995) 351-364
9. Lander H.M., Milbank A.J., Tauras J.M., Hajjar D.P., Hempstead B.L., Schwartz G.D., Kraemer R.T., Mirza U.A., Chait B.T., Burk S.C., and Quilliam L.A. Redox regulation of cell signalling. Nature 381 (1996) 380-381
10. Wojciak-Stothard B., Tsang L.Y., and Haworth S.G. Rac and Rho play opposing roles in the regulation of hypoxia/reoxygenation-induced permeability changes in pulmonary artery endothelial cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 288 (2005) L749-L760
11. Haendeler J., Hoffmann J., Brandes R.P., Zeiher A.M., and Dimmeler S. Hydrogen peroxide triggers nuclear export of telomerase reverse transcriptase via Src kinase family-dependent phosphorylation of tyrosine 707. Mol. Cell. Biol. 23 (2003) 4598-4610
12. Kodiha M., Chu A., Matusiewicz N., and Stochaj U. Multiple mechanisms promote the inhibition of classical nuclear import upon exposure to severe oxidative stress. Cell Death Differ. 11 (2004) 862-874
13. Miyamoto Y., Saiwaki T., Yamashita J., Yasuda Y., Kotera I., Shibata S., Shigeta M., Hiraoka Y., Haraguchi T., and Yoneda Y. Cellular stresses induce the nuclear accumulation of importin alpha and cause a conventional nuclear import block. J. Cell Biol. 165 (2004) 617-623
14. Lemaire S.D., Guillon B., Le Marechal P., Keryer E., Miginiac-Maslow M., and Decottignies P. New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 101 (2004) 7475-7480
15. Yan Y., Weaver V.M., and Blair I.A. Analysis of protein expression during oxidative stress in breast epithelial cells using a stable isotope labeled proteome internal standard. J. Proteome Res. 4 (2005) 2007-2014
16. Yasuda Y., Miyamoto Y., Saiwakim T., and Yoneda Y. Mechanism of the stress-induced collapse of the Ran distribution. Exp. Cell Res. 312 (2006) 512-520
17. Quan X., Tsoulos P., Kuritzky A., Zhang R., and Stochaj U. The carrier Msn5p/Kap142p promotes nuclear export of the hsp70 Ssa4p and relocates in response to stress. Mol. Microbiol. 62 (2006) 592-609
18. Kodiha M., Tran D., Qian C., Morogan A., Presley J.F., Brown C.M., and Stochaj U. Oxidative stress mislocalizes and retains transport factor importin-alpha and nucleoporins Nup153 and Nup88 in nuclei where they generate high molecular mass complexes. Biochim. Biophys. Acta 1783 (2008) 405-418
19. Ras S-nitrosylation and kinetics of nitric oxide-mediated guanine nucleotide exchange. Biochemistry 43 (2004) 2314-2322
20. Schwartz S.E., and White W.H. Kinetics of reactive dissolution of nitrogen oxide in aqueous solution. Adv. Environ. Sci. Technol. 12 (1983) 1-116
21. Bibak N., Paul R.M., Freymann D.M., and Yaseen N.R. Purification of RanGDP, RanGTP, and RanGMPPNP by ion exchange chromatography. Anal. Biochem. 333 (2004) 57-64
22. Heo J., and Campbell S.L. Superoxide anion radical modulates the activity of Ras and Ras-related GTPases by a radical-based mechanism similar to that of nitric oxide. J. Biol. Chem. 280 (2005) 12438-12445
23. Heo J., Prutzman K.C., Mocanu V., and Campbell S.L. Mechanism of free radical nitric oxide-mediated Ras guanine nucleotide dissociation. J. Mol. Biol. 346 (2005) 1423-1440
24. Heo J., and Campbell S.L. Mechanism of redox-mediated guanine nucleotide exchange on redox-active Rho GTPases. J. Biol. Chem. 280 (2005) 31003-31010
25. Ford E., Hughes M., and Wardman P. Kinetics of the reactions of nitrogen dioxide with glutathione, cysteine, and uric acid at physiological pH Free. Radic. Biol. Med. 32 (2002) 1314-1323
26. Jourd'heuil D., Jourd'heuil F., and Feelisch M. Oxidation and nitrosation of thiols at low micromolar exposure to nitric oxide. Evidence for a free radical mechanism. J. Biol. Chem. 278 (2003) 15720-15726
27. Heo J., and Campbell S.L. Ras regulation by reactive oxygen and nitrogen species. Biochemistry 45 (2006) 2200-2210
28. Heo J., Raines K.W., Mocanu V., and Campbell S.L. Redox regulation of RhoA. Biochemistry 45 (2006) 14481-14489
29. Stewart M., Kent H.M., and McCoy A.J. The structure of the Q69L mutant of GDP-Ran shows a major conformational change in the switch II loop that accounts for its failure to bind nuclear transport factor 2 (NTF2). J. Mol. Biol. 284 (1998) 1517-1527
30. Stubbe J., and van der Donk W.A. Protein radicals in enzyme catalysis. Chem. Rev. 98 (1998) 705-762
31. Pai E.F., Kabsch W., Krengel U., Holmes K.C., John J., and Wittinghofer A. Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature 341 (1989) 209-214
32. Brunger A.T., Milburn M.V., Tong L., deVos A.M., Jancarik J., Yamaizumi Z., Nishimura S., Ohtsuka E., and Kim S.H. Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain. Proc. Natl. Acad. Sci. USA 87 (1990) 4849-4853
33. Hirshberg M., Stockley R.W., Dodson G., and Webb M.R. The crystal structure of human rac1 a member of the rho-family complexed with a GTP analogue. Nat. Struct. Biol. 4 (1997) 147-152
34. Feltham J.L., Dotsch V., Raza S., Manor D., Cerione R.A., Sutcliffe M.J., Wagner G., and Oswald R.E. Definition of the switch surface in the solution structure of Cdc42Hs. Biochemistry 36 (1997) 8755-8766
35. Ihara K., Muraguchi S., Kato M., Shimizu T., Shirakawa M., Kuroda S., Kaibuchi K., and Hakoshima T. Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue. J. Biol. Chem. 273 (1998) 9656-9666
36. Graham T.E., Key T.A., Kilpatrick K., and Dorin R.I. Dexras1/AGS-1, a steroid hormone-induced guanosine triphosphate-binding protein, inhibits 3′,5′-cyclic adenosine monophosphate-stimulated secretion in AtT-20 corticotroph cells. Endocrinology 142 (2001) 2631-2640
37. Jaffrey S.R., Fang M., and Snyder S.H. Nitrosopeptide mapping: a novel methodology reveals s-nitrosylation of dexras1 on a single cysteine residue. Chem. Biol. 9 (2002) 1329-1335
38. Falk J.D., Vargiu P., Foye P.E., Usui H., Perez J., Danielson P.E., Lerner D.L., Bernal J., and Sutcliffe J.G. Rhes: a striatal-specific Ras homolog related to Dexras1. J. Neurosci. Res. 57 (1999) 782-788
39. Vargiu P., Morte B., Manzano J., Perez J., de Abajo R., Gregor Sutcliffe J., and Bernal J. Thyroid hormone regulation of rhes, a novel Ras homolog gene expressed in the striatum. Brain Res. Mol. Brain Res. 94 (2001) 1-8
40. Spano D., Branchi I., Rosica A., Pirro M.T., Riccio A., Mithbaokar P., Affuso A., Arra C., Campolongo P., Terracciano D., Macchia V., Bernal J., Alleva E., and Di Lauro R. Rhes is involved in striatal function. Mol. Cell. Biol. 24 (2004) 5788-5796