Review
Ero1 and redox homeostasis in the endoplasmic reticulum

https://doi.org/10.1016/j.bbamcr.2007.12.011Get rights and content
Under an Elsevier user license
open archive

Abstract

Living cells must be able to respond to physiological and environmental fluctuations that threaten cell function and viability. A cellular event prone to disruption by a wide variety of internal and external perturbations is protein folding. To ensure protein folding can proceed under a range of conditions, the cell has evolved transcriptional, translational, and posttranslational signaling pathways to maintain folding homeostasis during cell stress. This review will focus on oxidative protein folding in the endoplasmic reticulum (ER) and will discuss the features of the main facilitator of biosynthetic disulfide bond formation, Ero1. Ero1 plays an essential role in setting the redox potential in the ER and regulation of Ero1 activity is central to maintain redox homeostasis and proper ER folding activity.

Keywords

Ero1
Ero1p
Flavoprotein
Oxidase
Sulfhydryl oxidase
Chaperone
Disulfide
Thiol
Oxidation
Reduction
Cysteine
PDI
Pdi1p
Redox
Endoplasmic reticulum
ER
Protein folding
Oxidative folding
Disulfide bond formation
Glutathione
Reactive oxygen species
ROS
Oxidative stress
Posttranslational modification
Posttranslation regulation

Cited by (0)