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Article

Dynamic regulation of Ero1α and peroxiredoxin 4 localization in the secretory pathway.

The Journal of biological chemistry - 11 Oct 2013

Kakihana Taichi, Araki Kazutaka, Vavassori Stefano, Iemura Shun-ichiro, Cortini Margherita, Fagioli Claudio, Natsume Tohru, Sitia Roberto, Nagata Kazuhiro

Abstract excerpt

In the early secretory compartment (ESC), a network of chaperones and enzymes assists oxidative folding of nascent proteins. Ero1 flavoproteins oxidize protein disulfide isomerase (PDI), generating H2O2 as a byproduct. Peroxiredoxin 4 (Prx4) can utilize luminal H2O2 to oxidize PDI, thus favoring oxidative folding while limiting oxidative stress. Interestingly, neither ER oxidase contains known ER retention...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 23979138
DOI: 10.1074/jbc.M113.467845
PMCID: PMC3795256

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dynamic regulation of Ero1α and peroxiredoxin 4 localization in the secretory pathway.PMID 23979138Read ↗

PRDX4, an endoplasmic reticulum-localized peroxiredoxin at the crossroads between enzymatic oxidative protein folding and nonenzymatic protein oxidation.Semantic proximity Read ↗

Manipulation of oxidative protein folding and PDI redox state in mammalian cells.Semantic proximity Read ↗

Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway.Semantic proximity Read ↗

Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.Semantic proximity Read ↗

Biochemical basis of oxidative protein folding in the endoplasmic reticulum.Semantic proximity Read ↗

Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta.Semantic proximity Read ↗

A di-arginine motif contributes to the ER localization of the type I transmembrane ER oxidoreductase TMX4.Semantic proximity Read ↗

TMX5/TXNDC15, a natural trapping mutant of the PDI family is a client of the proteostatic factor ERp44.Semantic proximity Read ↗

Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum.Semantic proximity Read ↗

Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum.Semantic proximity Read ↗

Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.Semantic proximity Read ↗

Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1.Semantic proximity Read ↗

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