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

Trends Biochem Sci. 2009 Feb;34(2):85-96. doi: 10.1016/j.tibs.2008.11.002. Epub 2009 Jan 8.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Bacterial Proteins / metabolism
  • Glutathione / metabolism*
  • Humans
  • Models, Biological
  • Oxidation-Reduction
  • Oxidative Stress
  • Protein Folding
  • Protein Processing, Post-Translational / physiology*
  • RNA Stability
  • Signal Transduction


  • Bacterial Proteins
  • Glutathione