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- W2101573004 abstract "Glutathione contributes to thiol-redox control and to extra-mitochondrial iron-sulphur cluster (ISC) maturation. To determine the physiological importance of these functions and sort out those that account for the GSH requirement for viability, we performed a comprehensive analysis of yeast cells depleted of or containing toxic levels of GSH. Both conditions triggered an intense iron starvation-like response and impaired the activity of extra-mitochondrial ISC enzymes but did not impact thiol-redox maintenance, except for high glutathione levels that altered oxidative protein folding in the endoplasmic reticulum. While iron partially rescued the ISC maturation and growth defects of GSH-depleted cells, genetic experiments indicated that unlike thioredoxin, glutathione could not support by itself the thiol-redox duties of the cell. We propose that glutathione is essential by its requirement in ISC assembly, but only serves as a thioredoxin backup in cytosolic thiol-redox maintenance. Glutathione-high physiological levels are thus meant to insulate its cytosolic function in iron metabolism from variations of its concentration during redox stresses, a model challenging the traditional view of it as prime actor in thiol-redox control." @default.
- W2101573004 created "2016-06-24" @default.
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- W2101573004 date "2011-04-08" @default.
- W2101573004 modified "2023-10-18" @default.
- W2101573004 title "Glutathione revisited: a vital function in iron metabolism and ancillary role in thiol-redox control" @default.
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- W2101573004 doi "https://doi.org/10.1038/emboj.2011.105" @default.
- W2101573004 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3098478" @default.
- W2101573004 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21478822" @default.
- W2101573004 hasPublicationYear "2011" @default.
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