Manipulation of oxidative protein folding and PDI redox state in mammalian cells.

doi:10.1093/emboj/20.22.6288

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Article

Manipulation of oxidative protein folding and PDI redox state in mammalian cells.

The EMBO journal - 15 Nov 2001

Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R

Abstract excerpt

In the endoplasmic reticulum (ER), disulfide bonds are simultaneously formed in nascent proteins and removed from incorrectly folded or assembled molecules. In this compartment, the redox state must be, therefore, precisely regulated. Here we show that both human Ero1-Lalpha and Ero1-Lbeta (hEROs) facilitate disulfide bond formation in immunoglobulin subunits by selectively oxidizing PDI. Disulfide bond formation...

Topics

Amino Acid Motifs
Animals
Blotting, Western
Cell Line
Cysteine
Disulfides
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum
HeLa Cells
Humans
Immunoglobulin G
Membrane Glycoproteins
Models, Biological
Mutation

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Oxidation-Reduction

Oxidoreductases

Oxidoreductases Acting on Sulfur Group Donors

Oxygen

Source

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Identifiers

PMID: 11707400
DOI: 10.1093/emboj/20.22.6288
PMCID: PMC125306

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