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

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

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 condit...

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Bibliographic Details
Main Authors: Henning G. Hansen, Cecilie L. Søltoft, Jonas D. Schmidt, Julia Birk, Christian Appenzeller‑Herzog, Lars Ellgaard
Format: Article
Language:English
Published: Portland Press, Biochemical Society 2014-03-01
Series:Bioscience Reports
Subjects:
disulfide-bond formation
endoplasmic reticulum oxidoreductin-1 (Ero1)
redox regulation
unfolded protein response (UPR)
Online Access:http://www.bioscirep.org/bsr/034/e103/bsr034e103.htm

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http://www.bioscirep.org/bsr/034/e103/bsr034e103.htm

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