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Article

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

Life science alliance - 1 Dec 2024

Soldà Tatiana, Galli Carmela, Guerra Concetta, Hoefner Carolin, Molinari Maurizio

Abstract excerpt

The ER is the organelle of nucleated cells that produces lipids, sugars, and proteins. More than 20 ER-resident members of the protein disulfide isomerase (PDI) family regulate formation, isomerization, and disassembly of covalent bonds in newly synthesized polypeptides. The PDI family includes few membrane-bound members. Among these, TMX1, TMX2, TMX3, TMX4, and TMX5 belong to the thioredoxin-related...

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Identifiers

PMID: 39348940
DOI: 10.26508/lsa.202403047
PMCID: PMC11443168

Genes

ERAP1
SUMF1
TMX1
TMX2
TMX3
TMX4
TXNDC15

Provenance

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Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

TMX5/TXNDC15, a natural trapping mutant of the PDI family is a client of the proteostatic factor ERp44.PMID 39348940Read ↗

ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER.Semantic proximity Read ↗

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

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

Dynamic regulation of Ero1α and peroxiredoxin 4 localization in the secretory pathway.Semantic proximity Read ↗

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

The Highly Dynamic Nature of ERdj5 Is Key to Efficient Elimination of Aberrant Protein Oligomers through ER-Associated Degradation.Semantic proximity Read ↗

The ER Thioredoxin-Related Transmembrane Protein TMX2 Controls Redox-Mediated Tethering of ER-Mitochondria Contacts (ERMCS)Semantic proximity Read ↗

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

Loss of the oxidative stress sensor NPGPx compromises GRP78 chaperone activity and induces systemic disease.Semantic proximity Read ↗

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

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