Glutathione- and non-glutathione-based oxidant control in the endoplasmic reticulum
نویسندگان
چکیده
منابع مشابه
Glutathione- and non-glutathione-based oxidant control in the endoplasmic reticulum.
The redox-active tripeptide glutathione is an endogenous reducing agent that is found in abundance and throughout the cell. In the endoplasmic reticulum (ER), the ratio of glutathione to glutathione disulfide is lower compared with non-secretory organelles. This relatively oxidizing thiol-disulfide milieu is essential for the oxidative folding of nascent proteins in the ER and, at least in part...
متن کاملEndoplasmic reticulum : Reduced and oxidized glutathione
6 Division of Molecular and Systems Toxicology, Department of Pharmaceutical 7 Sciences, University of Basel, 4056 Basel, Switzerland 8 2 Swiss Center for Applied Human Toxicology, University of Basel, 4056 Basel, 9 Switzerland 10 3 INRES – Chemical Signalling, University of Bonn, 53113 Bonn, Germany 11 4 Department of Biology, University of Copenhagen, 2200 Copenhagen N, Denmark 12 5 D...
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Many proteins of the secretory pathway contain disulfide bonds that are essential for structure and function. In the endoplasmic reticulum (ER), Ero1 alpha and Ero1 beta oxidize protein disulfide isomerase (PDI), which in turn transfers oxidative equivalents to newly synthesized cargo proteins. However, oxidation must be limited, as some reduced PDI is necessary for disulfide isomerization and ...
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Glutathione is a ubiquitous molecule found in all parts of the cell where it fulfils a range of functions from detoxification to protection from oxidative damage. It provides the main redox buffer for cells and as such has been implicated in the formation of native disulphide bonds. However, the discovery of the enzyme Ero1 has called into question the exact role of glutathione in this process....
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Protein folding homeostasis in the endoplasmic reticulum (ER) requires efficient protein thiol oxidation, but also relies on a parallel reductive process to edit disulfides during the maturation or degradation of secreted proteins. To critically examine the widely held assumption that reduced ER glutathione fuels disulfide reduction, we expressed a modified form of a cytosolic glutathione-degra...
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ژورنال
عنوان ژورنال: Journal of Cell Science
سال: 2011
ISSN: 1477-9137,0021-9533
DOI: 10.1242/jcs.080895