Human ER Oxidoreductin-1α (Ero1α) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase.

ABSTRACT: In the mammalian endoplasmic reticulum, oxidoreductin-1α (Ero1α) generates protein disulfide bonds and transfers them specifically to canonical protein-disulfide isomerase (PDI) to sustain oxidative protein folding. This oxidative process is coupled to the reduction of O₂ to H₂O₂ on the bound flavin adenine dinucleotide cofactor. Because excessive thiol oxidation and H₂O₂ generation cause cell death, Ero1α activity must be properly regulated. In addition to the four catalytic cysteines (Cys⁹⁴, Cys⁹⁹, Cys¹⁰⁴, and Cys¹³¹) that are located in the flexible active site region, the Cys²⁰⁸-Cys²⁴¹ pair located at the base of another flexible loop is necessary for Ero1α regulatio

SUBMITTER: Kanemura S 

PROVIDER: S-EPMC5104921 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature