Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262.

ABSTRACT: In the ER (endoplasmic reticulum) of human cells, disulfide bonds are predominantly generated by the two isoforms of Ero1 (ER oxidoreductin-1): Ero1α and Ero1β. The activity of Ero1α is tightly regulated through the formation of intramolecular disulfide bonds to help ensure balanced ER redox conditions. Ero1β is less tightly regulated, but the molecular details underlying control of activity are not as well characterized as for Ero1α. Ero1β contains an additional cysteine residue (Cys²⁶²), which has been suggested to engage in an isoform-specific regulatory disulfide bond with Cys¹⁰⁰ However, we show that the two regulatory disulfide bonds in Ero1α are likely conserved in Ero1β (Cys⁹⁰-Cys¹³⁰ and Cys⁹⁵-Cys¹⁰⁰). Molecular mode

SUBMITTER: Hansen HG 

PROVIDER: S-EPMC3971451 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature