How Are Proteins Reduced in the Endoplasmic Reticulum?

Overview

Journal Trends Biochem Sci

Specialty Biochemistry

Date 2017 Nov 21

PMID 29153511

Citations 51

Authors

Lars Ellgaard

Carolyn S Sevier

Neil J Bulleid

Affiliations

Soon will be listed here.

Abstract

The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for protein folding, degradation, chaperone function, and the ER stress response. Our understanding of this process is generally poor but progress has been made. Enzymes performing the initial reduction of client proteins, as well as the ultimate electron donor in the pathway, have been identified. Most recently, a role for the cytosol in ER protein reduction has been revealed. Nevertheless, how reducing equivalents are transferred from the cytosol to the ER lumen remains an open question. We review here why proteins are reduced in the ER, discuss recent data on catalysis of steps in the pathway, and consider the implications for redox homeostasis within the early secretory pathway.

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