S-Glutathionylation

S-Glutathionylation is the posttranslational modification of protein cysteine residues by the addition of glutathione, the most abundant and important low-molecular-mass thiol within most cell types.^[1]

Protein S-glutathionylation is involved in the following:

oxidative stress^[1]
nitrosative stress^[1]
preventing irreversible oxidation of protein thiols^[1]
control of cell-signalling pathways by modulating protein function ^[1]

Protein S-glutathionylation, which is reversible,^[2] entails formation of a mixed disulfide. It is one of a host of reactions of the cysteine residues.

References

1 2 3 4 5 Dalle-Donne, Isabella; Rossi, Ranieri; Colombo, Graziano; Giustarini, Daniela; Milzani, Aldo (2009). "Protein S-glutathionylation: A regulatory device from bacteria to humans". Trends in Biochemical Sciences. 34 (2): 85–96. doi:10.1016/j.tibs.2008.11.002. PMID 19135374.
↑ Musaogullari, Aysenur; Chai, Yuh-Cherng (2020). "Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease". International Journal of Molecular Sciences. 21 (21): 8113. doi:10.3390/ijms21218113. PMC 7663550. PMID 33143095.

[dalle-1] 1 2 3 4 5 Dalle-Donne, Isabella; Rossi, Ranieri; Colombo, Graziano; Giustarini, Daniela; Milzani, Aldo (2009). "Protein S-glutathionylation: A regulatory device from bacteria to humans". Trends in Biochemical Sciences. 34 (2): 85–96. doi:10.1016/j.tibs.2008.11.002. PMID 19135374.

[2] Musaogullari, Aysenur; Chai, Yuh-Cherng (2020). "Redox Regulation by Protein S-Glutathionylation: From Molecular Mechanisms to Implications in Health and Disease". International Journal of Molecular Sciences. 21 (21): 8113. doi:10.3390/ijms21218113. PMC 7663550. PMID 33143095.

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