Ontology highlight
ABSTRACT:
SUBMITTER: Konno T
PROVIDER: S-EPMC4621842 | biostudies-other | 2015 Oct
REPOSITORIES: biostudies-other
Konno Tasuku T Pinho Melo Eduardo E Lopes Carlos C Mehmeti Ilir I Lenzen Sigurd S Ron David D Avezov Edward E
The Journal of cell biology 20151001 2
The endoplasmic reticulum (ER)-localized peroxiredoxin 4 (PRDX4) supports disulfide bond formation in eukaryotic cells lacking endoplasmic reticulum oxidase 1 (ERO1). The source of peroxide that fuels PRDX4-mediated disulfide bond formation has remained a mystery, because ERO1 is believed to be a major producer of hydrogen peroxide (H2O2) in the ER lumen. We report on a simple kinetic technique to track H2O2 equilibration between cellular compartments, suggesting that the ER is relatively isolat ...[more]