Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5646
Title: Protein S-glutathionylation: a regulatory device from bacteria to humans.
Authors: DALLE DONNE, I
Rossi, Ranieri 
Colombo, R
Giustarini, Daniela 
Milzani, A.
Issue Date: 2009
Project: None 
Journal: TRENDS IN BIOCHEMICAL SCIENCES
Abstract: 
S-Glutathionylation is the specific post-translational modification of protein cysteine residues by the addition of the tripeptide glutathione, the most abundant and important low-molecular-mass thiol within most cell types. Protein S-glutathionylation is promoted by oxidative or nitrosative stress but also occurs in unstressed cells. It can serve to regulate a variety of cellular processes by modulating protein function and to prevent irreversible oxidation of protein thiols. Recent findings support an essential role for S-glutathionylation in the control of cell-signalling pathways associated with viral infections and with tumour necrosis factor-(-induced apoptosis. Glyceraldehyde-3-phosphate dehydrogenase has recently been implicated in the regulation of endothelin-1 synthesis by a novel, S-glutathionylation-based mechanism involving messenger RNA stability. Moreover, recent studies have identified S-glutathionylation as a redox signalling mechanism in plants.
Description: 
24136
URI: http://hdl.handle.net/20.500.12779/5646
ISSN: 0968-0004
DOI: 10.1016/j.tibs.2008.11.002
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