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.

DALLE DONNE, I., Rossi, R., Colombo, R., Giustarini, D., Milzani, A. (2009). Protein S-glutathionylation: a regulatory device from bacteria to humans. TRENDS IN BIOCHEMICAL SCIENCES, 34, 85-96 [10.1016/j.tibs.2008.11.002].

Protein S-glutathionylation: a regulatory device from bacteria to humans.

ROSSI, RANIERI;GIUSTARINI, DANIELA;
2009-01-01

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.
2009
DALLE DONNE, I., Rossi, R., Colombo, R., Giustarini, D., Milzani, A. (2009). Protein S-glutathionylation: a regulatory device from bacteria to humans. TRENDS IN BIOCHEMICAL SCIENCES, 34, 85-96 [10.1016/j.tibs.2008.11.002].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11365/24885
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