Oxidative protein folding in the mammalian endoplasmic reticulum.

Abstract:

:Native disulphide bonds are essential for the structure and function of many membrane and secretory proteins. Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which includes protein disulphide isomerase (PDI), ERp57, ERp72, P5 and PDIR. This review will discuss how these enzymes are maintained in either an oxidized redox state that allows them to form disulphide bonds in substrate proteins or a reduced form that allows them to perform isomerization and reduction reactions, how these opposing pathways may co-exist within the same compartment and why so many oxidoreductases exist when PDI alone can perform all three of these functions.

journal_name

Biochem Soc Trans

authors

Jessop CE,Chakravarthi S,Watkins RH,Bulleid NJ

doi

10.1042/BST0320655

keywords:

subject

Has Abstract

pub_date

2004-11-01 00:00:00

pages

655-8

issue

Pt 5

eissn

0300-5127

issn

1470-8752

pii

BST0320655

journal_volume

32

pub_type

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