Endoplasmic Reticulum Oxidoreductin 1-Lβ (ERO1-Lβ), a Human Gene Induced in the Course of the Unfolded Protein Response* 210

By M. Pagani, M. Fabbri, C. Benedetti, A. Fassio, S. Pilati, N. Bulleid, A. Cabibbo, Roberto Sitia. Journal of Biological Chemistry, 2000

250 citations recorded by the source corpus.

Oxidative conditions must be generated in the endoplasmic reticulum (ER) to allow disulfide bond formation in secretory proteins. A family of conserved genes, termed EROfor ER oxidoreductins, plays a key role in this process. We have previously described the human gene ERO1-L, which complements several phenotypic traits of the yeast thermo-sensitive mutant ero1-1 (Cabibbo, A., Pagani, M., Fabbri, M., Rocchi, M., Farmery, M. R., Bulleid, N. J., and Sitia, R. (2000)J. Biol. Chem. 275, 4827–4833). Here, we report the cloning and characterization of a novel human member of this family,ERO1-Lβ. Immunofluorescence, endoglycosidase sensitivity, and in vitro translation/translocation assays reveal that the products of the ERO1-Lβ gene are primarily localized in the ER of mammalian cells. The ability to allow growth at 37 °C and to alleviate the “unfolded protein response” when expressed inero1-1 cells indicates that ERO1-Lβ is involved also in generating oxidative conditions in the ER. ERO1-L and ERO1-Lβ display different tissue distributions. Furthermore, only ERO1-Lβ transcripts are induced in the course of the unfolded protein response. Our results suggest a complex regulation of ER redox homeostasis in mammalian cells.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/3427aad8dd37d5bb39dfae05f2ffa0817f69066f

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In Cell Biology

1. D. Ron
2. R. Kaufman
3. H. Harding
4. S. Oyadomari
5. S. Marciniak
6. I. Novoa
7. Yuhong Zhang
8. Chi Y. Yun

In Molecular Biology

1. D. Ron
2. H. Harding
3. R. Kaufman
4. I. Novoa
5. Yuhong Zhang
6. S. Marciniak
7. S. Oyadomari
8. Chi Y. Yun

Citations in the corpus

• CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. (2004, background): “Furthermore, cells have a second isoform, ERO1 (Pagani et al. 2000), whose induction by ER stress is unaffected by the CHOP mutation.”
• The role for endoplasmic reticulum stress in diabetes mellitus. (2008, background): “PDI is oxidized by Ero1 (35) and - (36) into a disulfide donor, whereas reduced PDI can isomerize disulfide bonds in client proteins.”
• Protein quality control in the early secretory pathway (2008, background): “After transferring a disulfide bond to nascent proteins, PDI is re-oxidized by members of the Ero1 flavoprotein family (Frand and Kaiser, 1998; Pollard et al, 1998; Cabibbo et al, 2000; Pagani et al, 2000; Mezghrani et al, 2001).”
• Formation and transfer of disulphide bonds in living cells (2002, background): “Both Ero1-Lα and Ero1-Lα can complement the phenotypic defects associated with the yeast mutant ero1-1 strai”
• The changing faces of glutathione, a cellular protagonist. (2003, background): “Thus, ERO1B is likely to be under increased demand for disulfide formation in the secretory tissues where it is expressed compared to ERO1 homologs in other tissues.”