4.4 Article

Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides

Journal

MOLECULAR BIOLOGY OF THE CELL
Volume 26, Issue 19, Pages 3390-3400

Publisher

AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E15-05-0321

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Funding

  1. Foundation for Research on Neurodegenerative Diseases
  2. Swiss National Science Foundation
  3. Comel Foundation
  4. Wellcome Trust [88053]
  5. Biocenter Oulu
  6. Gelu Foundation
  7. BBSRC [BB/D00764X/1] Funding Source: UKRI
  8. Wellcome Trust [103720/Z/14/Z] Funding Source: Wellcome Trust
  9. Biotechnology and Biological Sciences Research Council [BB/D00764X/1] Funding Source: researchfish
  10. Wellcome Trust [103720/Z/14/Z] Funding Source: researchfish

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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.

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