title: Protein S-glutathionylation: a regulatory device from bacteria to humans.
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.
authors.affiliation: Department of Biology, University of Milan, via Celoria 26, I-20133, Milan, Italy. quack@unimi.it
authors.forename: Isabella
authors.initials: I
authors.lastname: Dalle-Donne
authors.forename: Ranieri
authors.initials: R
authors.lastname: Rossi
authors.forename: Graziano
authors.initials: G
authors.lastname: Colombo
authors.forename: Daniela
authors.initials: D
authors.lastname: Giustarini
authors.forename: Aldo
authors.initials: A
authors.lastname: Milzani
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D005978:Glutathione / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D017510:Protein Folding; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D020871:RNA Stability; D015398:Signal Transduction
chemical_list: D001426:Bacterial Proteins; D005978:Glutathione