Regulation of protein function by glutathionylation

Free Radic Res. 2005 Jun;39(6):573-80. doi: 10.1080/10715760500072172.

Abstract

The main function of reduced glutathione (GSH) is to protect from oxidative stress as a reactive oxygen scavenger. However, in the context of redox regulation, the ratio between GSH and its oxidized form (GSSG) determines the redox state of redox-sensitive cysteines in some proteins and, thus, acts as a signaling system. While GSH/GSSG can catalyze oxido-reduction of intra- and inter-chain disulfides by thiol-disulfide exchange, this review focuses on the formation of mixed disulfides between glutathione and proteins, also known as glutathionylation. The review discusses the regulatory role of this post-translational modification and the role of protein disulfide oxidoreductases (thioredoxin/thioredoxin reductase, glutaredoxin, protein disulfide isomerase) in the reversibility of this process.

Publication types

  • Review

MeSH terms

  • Animals
  • Disulfides / metabolism
  • Glutathione / metabolism*
  • Humans
  • Oxidation-Reduction
  • Oxidative Stress
  • Proteins / metabolism*

Substances

  • Disulfides
  • Proteins
  • Glutathione