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Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation.
Zhichao Liu1, Nicolas Rouhier1,2, Jérémy Couturier1,2
1Université de Lorraine, INRAE, IAM, F-54000 Nancy, France.
Hydrogen sulfide (H2S) signaling involves protein persulfidation, a key thiol modification. This review explores H2S pathways and the dual roles of thioredoxin and glutaredoxin systems in persulfidation and depersulfidation.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Signaling
Background:
- Protein persulfidation, the oxidative modification of cysteine residues to persulfides, is a primary mechanism for hydrogen sulfide (H2S) biological and signaling functions.
- Persulfidation acts as a crucial thiol-switching mechanism, akin to other reversible redox post-translational modifications.
Purpose of the Study:
- To review recent advances in physiological pathways of protein persulfidation.
- To discuss the potential dual roles of glutaredoxin (GRX) and thioredoxin (TRX) reducing systems in protein persulfidation and depersulfidation.
Main Methods:
- Literature review focusing on recent research in protein persulfidation.
- Analysis of the known reductase activities and H2S-related connections of GRX and TRX systems.
Main Results:
- Recent physiological pathways leading to protein persulfidation have been identified.
- The thioredoxin (TRX) and glutathione/glutaredoxin (GRX) reducing systems exhibit potential dual roles in both the addition and removal of persulfide groups on proteins.
Conclusions:
- Protein persulfidation is a significant redox modification mediated by hydrogen sulfide.
- The TRX and GRX systems are key players, capable of both facilitating and reversing protein persulfidation, highlighting their critical regulatory function.
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