Modifications of Cysteine Proteins Redox Status in Cell Signalling
A special issue of Antioxidants (ISSN 2076-3921). This special issue belongs to the section "Aberrant Oxidation of Biomolecules".
Deadline for manuscript submissions: closed (28 February 2021) | Viewed by 14547
Special Issue Editor
Interests: oxidative stress; protein thiolation; carbonyl metabolism; enzyme inhibition; diabetic complications; drug discovery
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Special Issue Information
Dear Colleagues,
A huge number of proteins, including enzymes, transcription factors and cytoskeletal proteins, may undergo changes in the redox status of their cysteines. These modifications, including glutathionylation (and the more general thiolation), often lead to stable protein-mixed disulphides or to a rearrangement into intra/intermolecular disulphides. Although the first evidence of protein-mixed disulphides dates back to the 1980s, exactly how they are generated is still not clear and, consequently, whether reduced or oxidized glutathione is involved. In addition, there is increasing evidence that proteins may contain cysteine in different oxidation states, such as cysteine sulphenic and sulphinic acid (through the occurrence of sulphenylation and sulphinylation processes, respectively), and that these modifications are reversible. In fact, specific catalysts of de-modification events, such as glutaredoxins for the reverse of glutathionylation and sulfiredoxins for the reverse of sulphenylation and sulphinylation, have been described. This evidence, together with the fact that such post-translational modifications often result in alterations of the functional properties of target proteins, strongly suggests that they may have a regulatory role. Along with the increase in experimental evidence, these proposals have been refined over the years and we are now at the point of a fascinating concept: the cellular “thiolstat”. This is based on the assumption that the different redox states observed for cysteine proteins may represent sensors for different extents of oxidative stress, which are consequently able to affect cell fate. However, the factors that play a role in promoting/catalyzing or hindering these modifications and de-modifications are still not fully clear and neither is the extent of reversibility or the actual significance of these modifications in terms of cell signaling.
We invite authors to contribute, with research articles or reviews, to shed light on the above points. Thus, this Special Issue welcomes submissions on all aspects related to modifications in the redox status of cysteine proteins, including (but not limited to) their role and occurrence in diseases, the characterization of enzymes able to catalyze both the modification and the de-modification steps, and the methodological approaches for detecting their occurrence.
Prof. Antonella Del Corso
Guest Editor
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Keywords
- Cysteine redox status
- Glutathionylation
- Thiolation
- Protein-mixed disulphides
- Sulfenylation
- Sulphinylation
- Glutaredoxin
- Sulfiredoxin
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