Ontology highlight
ABSTRACT:
SUBMITTER: Tsunoda S
PROVIDER: S-EPMC4109312 | biostudies-literature | 2014 Jul
REPOSITORIES: biostudies-literature
Tsunoda Satoshi S Avezov Edward E Zyryanova Alisa A Konno Tasuku T Mendes-Silva Leonardo L Pinho Melo Eduardo E Harding Heather P HP Ron David D
eLife 20140729
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-degrading enzyme, ChaC1, in the ER lumen. ChaC1(CtoS) purged the ER of glutathione eliciting the expected ki ...[more]