201
Views
5
CrossRef citations to date
0
Altmetric
Original Article

Prediction of glutathionylation sites in proteins using minimal sequence information and their experimental validation

, , &
Pages 1011-1021 | Received 05 Feb 2016, Accepted 20 Jul 2016, Published online: 22 Aug 2016

References

  • Lu S, Fan SB, Yang B, Li YX, Meng JM, Wu L, et al. Mapping native disulfide bonds at a proteome scale. Nat Methods 2015;12:329–331.
  • Checker R, Gambhir L, Sharma D, Kumar M, Sandur SK. Plumbagin induces apoptosis in lymphoma cells via oxidative stress mediated glutathionylation and inhibition of mitogen-activated protein kinase phosphatases (MKP1/2). Cancer Lett 2015;357:265–278.
  • Gambhir L, Checker R, Thoh M, Patwardhan RS, Sharma D, Kumar M, Sandur SK. 1,4-Naphthoquinone, a pro-oxidant, suppresses immune responses via KEAP-1 glutathionylation. Biochem Pharmacol 2014;88:95–105.
  • Johnstone VP, Hool LC. Glutathionylation of the L-type Ca2+ channel in oxidative stress-induced pathology of the heart. Int J Mol Sci 2014;15:19203–19225.
  • Juel C. Oxidative stress (glutathionylation) and Na, K-ATPase activity in rat skeletal muscle. PLoS One 2014;9:e110514.
  • Dalle-Donne I, Rossi R, Colombo G, Giustarini D, Milzani A. Protein S-glutathionylation: a regulatory device from bacteria to humans. Trends Biochem Sci 2009;34:85–96.
  • Prinarakis E, Chantzoura E, Thanos D, Spyrou G. S-glutathionylation of IRF3 regulates IRF3-CBP interaction and activation of the IFN beta pathway. EMBO J 2008;27:865–875.
  • Pan S, Berk BC. Glutathiolation regulates tumor necrosis factor-alpha-induced caspase-3 cleavage and apoptosis: key role for glutaredoxin in the death pathway. Circ Res 2007;100:213–219.
  • Demasi M, Silva GM, Netto LE. 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J Biol Chem 2003;278:679–685.
  • Silva GM, Netto LE, Simoes V, Santos LF, Gozzo FC, Demasi MA, et al. Redox control of 20S proteasome gating. Antioxid Redox Signal 2012;16:1183–1194.
  • Xiong Y, Uys JD, Tew KD, Townsend DM. S-glutathionylation: from molecular mechanisms to health outcomes. Antioxid Redox Signal 2011;15:233–270.
  • Pastore A, Piemonte F. Protein glutathionylation in cardiovascular diseases. Int J Mol Sci 2013;14:20845–20876.
  • Sabens Liedhegner EA, Gao XH, Mieyal JJ. Mechanisms of altered redox regulation in neurodegenerative diseases-focus on S-glutathionylation. Antioxid Redox Signal 2012;16:543–566.
  • Dalle-Donne I, Milzani A, Gagliano N, Colombo R, Giustarini D, Rossi R. Molecular mechanisms and potential clinical significance of S-glutathionylation. Antioxid Redox Signal 2008;10:445–473.
  • Mieyal JJ, Gallogly MM, Qanungo S, Sabens EA, Shelton MD. Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid Redox Signal 2008;10:1941–1988.
  • Grek CL, Zhang J, Manevich Y, Townsend DM, Tew KD. Causes and consequences of cysteine S-glutathionylation. J Biol Chem 2013;288:26497–26504.
  • Townsend DM, Manevich Y, He L, Hutchens S, Pazoles CJ, Tew KD. Novel role for glutathione S-transferase pi. Regulator of protein S-Glutathionylation following oxidative and nitrosative stress. J Biol Chem 2009;284:436–445.
  • Nulton-Persson AC, Starke DW, Mieyal JJ, Szweda LI. Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status. Biochemistry 2003;42:4235–4242.
  • Sun R, Eriksson S, Wang L. Oxidative stress induced S-glutathionylation and proteolytic degradation of mitochondrial thymidine kinase 2. J Biol Chem 2012;287:24304–24312.
  • Drose S, Brandt U, Wittig I. Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation. Biochim Biophys Acta 2014;1844:1344–1354.
  • Mailloux RJ, Willmore WG. S-glutathionylation reactions in mitochondrial function and disease. Front Cell Dev Biol 2014;2:68.
  • Gallogly MM, Mieyal JJ. Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr Opin Pharmacol 2007;7:381–91.
  • Carvalho AN, Marques C, Guedes RC, Castro-Caldas M, Rodrigues E, van Horssen J, Gama MJ. S-Glutathionylation of Keap1: a new role for glutathione S-transferase pi in neuronal protection. FEBS Lett 2016;590:1455–1466.
  • Hamnell-Pamment Y, Lind C, Palmberg C, Bergman T, Cotgreave IA. Determination of site-specificity of S-glutathionylated cellular proteins. Biochem Biophys Res Commun 2005;332:362–369.
  • Su D, Gaffrey MJ, Guo J, Hatchell KE, Chu RK, Clauss TR, et al. Proteomic identification and quantification of S-glutathionylation in mouse macrophages using resin-assisted enrichment and isobaric labeling. Free Radic Biol Med 2014;67:460–470.
  • Sun C, Shi ZZ, Zhou X, Chen L, Zhao XM. Prediction of S-glutathionylation sites based on protein sequences. PLoS One 2013;8:e55512.
  • Zhao X, Ning Q, Ai M, Chai H, Yin M. PGluS: prediction of protein S-glutathionylation sites with multiple features and analysis. Mol Biosyst 2015;11:923–929.
  • Chen YJ, Lu CT, Huang KY, Wu HY, Lee TY. GSHSite: exploiting an iteratively statistical method to identify s-glutathionylation sites with substrate specificity. PLoS One 2015;10:e0118752.
  • Chen YJ, Lu CT, Lee TY. dbGSH: a database of S-glutathionylation. Bioinformatics 2014;30:2386–2368.
  • Chardonnet S, Sakr S, Cassier-Chauvat C, Le Maréchal P, Chauvat F, Lemaire SD, Decottignies P. First proteomic study of S-glutathionylation in cyanobacteria. J Proteome Res 2015;14:59–71.
  • Cremers CM, Jakob U. Oxidant sensing by reversible disulfide bond formation. J Biol Chem 2013;288:26489–26496.
  • Luo D, Smith SW, Anderson BD. Kinetics and mechanism of the reaction of cysteine and hydrogen peroxide in aqueous solution. J Pharm Sci 2005;94:304–16.
  • Marino SM, Gladyshev VN. Cysteine function governs its conservation and degeneration and restricts its utilization on protein surfaces. J Mol Biol 2010;404:902–916.
  • Grauschopf U, Winther JR, Korber P, Zander T, Dallinger P, Bardwell JC. Why is DsbA such an oxidizing disulfide catalyst? Cell 1995;83:947–955.
  • Chiang BY, Chou CC, Hsieh FT, Gao S, Lin JC, Lin SH, et al. In vivo tagging and characterization of S-glutathionylated proteins by a chemoenzymatic method. Angew Chem Int Ed Engl 2012;51:5871–5875.
  • Curmi PA, Andersen SS, Lachkar S, Gavet O, Karsenti E, Knossow M, Sobel A. The stathmin/tubulin interaction in vitro. J Biol Chem 1997;272:25029–25036.
  • Jourdain L, Curmi P, Sobel A, Pantaloni D, Carlier MF. Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules. Biochemistry 1997;36:10817–10821.
  • Steinmetz MO. Structure and thermodynamics of the tubulin-stathmin interaction. J Struct Biol 2007;158:137–47.
  • Niethammer P, Bastiaens P, Karsenti E. Stathmin-tubulin interaction gradients in motile and mitotic cells. Science 2004;303:1862–1866.
  • Hill CM, Libich DS, Harauz G. Assembly of tubulin by classic myelin basic protein isoforms and regulation by post-translational modification. Biochemistry 2005;44:16672–16683.
  • Kang EY, Ponzio M, Gupta PP, Liu F, Butensky A, Gutstein DE. Identification of binding partners for the cytoplasmic loop of connexin43: a novel interaction with β-tubulin. Cell Commun Adhes 2009;15:397–406.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.