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- W2200117718 abstract "The endoplasmic reticulum (ER) is the site of maturation for secretory and membrane proteins in eukaryotic cells. The lumen of the mammalian ER contains >20 members of the protein disulfide isomerase (PDI) superfamily, which ensure formation of the correct set of intramolecular and intermolecular disulfide bonds as crucial, rate-limiting reactions of the protein folding process. Components of the PDI superfamily may also facilitate dislocation of misfolded polypeptides across the ER membrane for ER-associated degradation (ERAD). The reasons for the high redundancy of PDI family members and the substrate features required for preferential engagement of one or the other are poorly understood. Here we show that TMX1, one of the few transmembrane members of the family, forms functional complexes with the ER lectin calnexin and preferentially intervenes during maturation of cysteine-containing, membrane-associated proteins while ignoring the same cysteine-containing ectodomains if not anchored at the ER membrane. As such, TMX1 is the first example of a topology-specific client protein redox catalyst in living cells." @default.
- W2200117718 created "2016-06-24" @default.
- W2200117718 creator A5008290085 @default.
- W2200117718 creator A5012945125 @default.
- W2200117718 creator A5016746605 @default.
- W2200117718 creator A5035366529 @default.
- W2200117718 date "2015-10-01" @default.
- W2200117718 modified "2023-09-30" @default.
- W2200117718 title "Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides" @default.
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- W2200117718 doi "https://doi.org/10.1091/mbc.e15-05-0321" @default.
- W2200117718 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4591685" @default.
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