Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation
The oxidative modification of specific cysteine residues to persulfides is thought to be the main way by which hydrogen sulfide (H<sub>2</sub>S) exerts its biological and signaling functions. Therefore, protein persulfidation represents an important thiol-switching mechanism as other rev...
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MDPI AG
2025-01-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/14/1/101 |
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| author | Zhichao Liu Nicolas Rouhier Jérémy Couturier |
| author_facet | Zhichao Liu Nicolas Rouhier Jérémy Couturier |
| author_sort | Zhichao Liu |
| collection | DOAJ |
| description | The oxidative modification of specific cysteine residues to persulfides is thought to be the main way by which hydrogen sulfide (H<sub>2</sub>S) exerts its biological and signaling functions. Therefore, protein persulfidation represents an important thiol-switching mechanism as other reversible redox post-translational modifications. Considering their reductase activity but also their connections with proteins that generate H<sub>2</sub>S and its related molecules, the glutaredoxin (GRX) and thioredoxin (TRX)-reducing systems have potential dual roles in both protein persulfidation and depersulfidation. In this review, we will first focus on recent advances describing the physiological pathways leading to protein persulfidation before discussing the dual roles of the physiological TRX and glutathione/GRX-reducing systems in protein persulfidation/depersulfidation. |
| format | Article |
| id | doaj-art-4a21d3c5849e4efb9798d590bcb24108 |
| institution | Kabale University |
| issn | 2076-3921 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj-art-4a21d3c5849e4efb9798d590bcb241082025-01-24T13:19:29ZengMDPI AGAntioxidants2076-39212025-01-0114110110.3390/antiox14010101Dual Roles of Reducing Systems in Protein Persulfidation and DepersulfidationZhichao Liu0Nicolas Rouhier1Jérémy Couturier2Université de Lorraine, INRAE, IAM, F-54000 Nancy, FranceUniversité de Lorraine, INRAE, IAM, F-54000 Nancy, FranceUniversité de Lorraine, INRAE, IAM, F-54000 Nancy, FranceThe oxidative modification of specific cysteine residues to persulfides is thought to be the main way by which hydrogen sulfide (H<sub>2</sub>S) exerts its biological and signaling functions. Therefore, protein persulfidation represents an important thiol-switching mechanism as other reversible redox post-translational modifications. Considering their reductase activity but also their connections with proteins that generate H<sub>2</sub>S and its related molecules, the glutaredoxin (GRX) and thioredoxin (TRX)-reducing systems have potential dual roles in both protein persulfidation and depersulfidation. In this review, we will first focus on recent advances describing the physiological pathways leading to protein persulfidation before discussing the dual roles of the physiological TRX and glutathione/GRX-reducing systems in protein persulfidation/depersulfidation.https://www.mdpi.com/2076-3921/14/1/101hydrogen sulfideprotein persulfidationthioredoxinglutaredoxinglutathionesulfurtransferase |
| spellingShingle | Zhichao Liu Nicolas Rouhier Jérémy Couturier Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation Antioxidants hydrogen sulfide protein persulfidation thioredoxin glutaredoxin glutathione sulfurtransferase |
| title | Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation |
| title_full | Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation |
| title_fullStr | Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation |
| title_full_unstemmed | Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation |
| title_short | Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation |
| title_sort | dual roles of reducing systems in protein persulfidation and depersulfidation |
| topic | hydrogen sulfide protein persulfidation thioredoxin glutaredoxin glutathione sulfurtransferase |
| url | https://www.mdpi.com/2076-3921/14/1/101 |
| work_keys_str_mv | AT zhichaoliu dualrolesofreducingsystemsinproteinpersulfidationanddepersulfidation AT nicolasrouhier dualrolesofreducingsystemsinproteinpersulfidationanddepersulfidation AT jeremycouturier dualrolesofreducingsystemsinproteinpersulfidationanddepersulfidation |