Abstract
It is the functioning of efficient cell signaling which is vital for the survival of cells, whether it is a simple prokaryote or a complex eukaryote, including both animals and plants. Over many years various components have been identified and recognized as crucial for the transduction of signals in cells, including small organic molecules and ions. Many of the mechanisms allow for a relatively rapid switching of signals, on or off, with common examples being the G proteins and protein phosphorylation. However, it has become apparent that other amino acid modifications are also vitally important. This includes reactions with nitric oxide, for example S-nitrosation (S-nitrosylation), and, of particular relevance here, oxidation of cysteine residues. Such oxidation will be dependent on the redox status of the intracellular environment in which that protein resides, and this will in turn be dictated by the presence of pro-oxidants and antioxidants, either produced by the cell itself or from the cell’s environment. Here, the chemistry of redox modification of amino acids is introduced, and a general overview of the role of redox in mediating signal transduction is given.
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References
Hancock JT (1997) Superoxide, hydrogen peroxide and nitric oxide as signalling molecules: their production and role in disease. Br J Biomed Sci 54:38–46
Dröge W (2002) Free Radicals in physiological control of cell function. Physiol Rev 82:47–95
Neill SJ, Desikan R, Hancock JT (2002) Hydrogen peroxide signalling. Curr Opin Plant Biol 5:388–395
Colavitti R, Finkel T (2005) Reactive oxygen species as mediators of cellular senescence. IUBMB Life 57:277–281
Hancock JT (2009) The role of redox mechanisms in cell signaling. Mol Biotechnol 43:162–166
Vanderauwera S, Zimmermann P, Rombauts S, Vandenbeele S, Langebartels C, Gruissem W, Inzé D, Van Breusegem F (2005) Genome-wide analysis of hydrogen peroxide–regulated gene expression in Arabidopsis reveals a high light-induced transcriptional cluster involved in anthocyanin biosynthesis. Plant Physiol 139:806–821
Ullrich V, Kissner R (2006) Redox signaling: bioinorganic chemistry at its best. J Inorg Biochem 100:2079–2086
Hancock JT, Whiteman M (2014) Hydrogen sulfide and cell signaling: team player or referee? Plant Physiol Biochem 78:37–42
Hancock JT (2016) Cell Signalling, 4th edn. Oxford University Press, Oxford
Neill SJ, Desikan R, Hancock JT (2003) Nitric oxide signalling in plants. New Phytol 159:11–35
Perazzolli M, Romero-Puertas MC, Delledonne M (2006) Modulation of nitric oxide bioactivity by plant haemoglobins. J Exp Bot 57:479–488
Salmeen A, Anderson JN, Myers MP, Meng TC, Hinks JA, Tonks NK, Barford D (2003) Redox regulation of protein tyrosine phosphatase 1B involves a novel sulfenyl-amide intermediate. Nature 423:769–773
Van Montfort RL, Congreve M, Tisi D, Carr R, Jhoti H (2003) Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423:773–777
Lindermayr C, Saalbach G, Durner J (2005) Proteomic identification of S-nitrosylated proteins in Arabidopsis. Plant Physiol 137:921–930
Sen N, Paul BD, Gadalla MM et al (2012) Hydrogen sulfide-linked sulfhydration of NF-κB mediates its antiapoptotic actions. Mol Cell 45:13–24
Dixon DP, Skipsey M, Grundy NM, Edwards R (2005) Stress-induced protein S-glutathionylation in Arabidopsis. Plant Physiol 138:2233–2244
Hancock J, Desikan R, Harrison J, Bright J, Hooley R, Neill S (2006) Doing the unexpected: proteins involved in hydrogen peroxide perception. J Exp Bot 57:1711–1718
Cho S-H, Lee C-C, Ahn Y, Kim H, Yang K-S, Lee S-R (2004) Redox regulation of PTEN and protein tyrosine phosphatase in H2O2-mediated cell signalling. FEBS Lett 560:7–13
Desikan R, Hancock JT, Bright J, Harrison J, Weir I, Hooley R, Neill SJ (2005) A novel role for ETR1: hydrogen peroxide signalling in stomatal guard cells. Plant Physiol 137:831–834
Hancock JT, Henson D, Nyirenda M, Desikan R, Harrison J, Lewis L, Hughes J, Neill SJ (2005) Proteomic identification of glyceraldehyde 3-phosphate dehydrogenase as an inhibitory target of hydrogen peroxide in Arabidopsis. Plant Physiol Biochem 43:828–835
Lee C, Lee SM, Mukhopadhyay P, Kim SJ, Lee SC, Ahn WS, Yu MH, Stroz G, Ryu SE (2004) Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path. Nat Struct Mol Biol 11:1179–1185
Zhang Y, Keszler A, Broniowska KA, Hogg N (2005) Characterization and application of the biotin-switch assay for the identification of S-nitrosated proteins. Free Radic Biol Med 38:871–881
Schürmann P, Jacquot JP (2000) Plant thioredoxin systems revisited. Annu Rev Plant Physiol Plant Mol Biol 51:371–400
Lemaire SD (2004) The glutaredoxin family in oxygenic photosynthetic organisms. Photosynth Res 79:305–318
Collin V, Lankemeyer P, Miginiac-Maslow M, Hirasawa M, Knaff DB, Dietz KJ, Issakidis-Bourguet E (2004) Characterization of plastidial thioredoxins belonging to the new y-type. Plant Physiol 136:4088–4095
Rouhier N, Gelhaye E, Sautiere PE, Brun A, Laurent P, Tagu D, Gerard J, De Fay E, Meyer Y, Jacquot JP (2001) Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor. Plant Physiol 127:1299–1309
Biteau B, Labarre J, Toledano MB (2003) ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425:980–984
Malik SI, Hussain A, Yun BW, Spoel SH, Loake GJ (2011) GSNOR-mediated de-nitrosylation in the plant defence response. Plant Sci 181:540–544
Yu M, Yun BW, Spoel SH, Loake GJ (2012) A sleigh ride through the SNO: regulation of plant immune function by protein S-nitrosylation. Curr Opin Plant Biol 15:424–430
Hancock JT (2003) The principles of cell signalling. In: Kumar S, Bentley PJ (eds) On Growth, Form and Computers. Academic, London
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Hancock, J.T. (2019). The Role of Redox in Signal Transduction. In: Hancock, J., Conway, M. (eds) Redox-Mediated Signal Transduction. Methods in Molecular Biology, vol 1990. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9463-2_1
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DOI: https://doi.org/10.1007/978-1-4939-9463-2_1
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