Ero1l

Summary

Gene Symbol: Ero1l
Description: ERO1-like (S. cerevisiae)
Alias: ERO1-L, Ero1a, ERO1-like protein alpha, ERO1-L-alpha, endoplasmic oxidoreductin-1-like protein, endoplasmic reticulum oxidation 1, endoplasmic reticulum oxidoreductase alpha, endoplasmic reticulum oxidoreductin-1-like protein, oxidoreductin-1-L-alpha
Species: mouse
Products:     Ero1l

Top Publications

  1. Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery M, Bulleid N, et al. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J Biol Chem. 2000;275:4827-33 pubmed
    ..ERO1-L is no longer functional when either one of the highly conserved Cys-394 or Cys-397 is mutated. These results strongly suggest that ERO1-L is involved in oxidative ER protein folding in mammalian cells. ..
  2. Marciniak S, Yun C, Oyadomari S, Novoa I, Zhang Y, Jungreis R, et al. CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Genes Dev. 2004;18:3066-77 pubmed
    ..CHOP deletion thus protects cells from ER stress by decreasing ER client protein load and changing redox conditions within the organelle. ..
  3. Zito E, Chin K, Blais J, Harding H, Ron D. ERO1-beta, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis. J Cell Biol. 2010;188:821-32 pubmed publisher
    ..Surprisingly, concomitant disruption of Ero1l, encoding the other ERO1 isoform, ERO1-alpha, does not exacerbate the ERO1-beta deficiency phenotype...
  4. May D, Itin A, Gal O, Kalinski H, Feinstein E, Keshet E. Ero1-L alpha plays a key role in a HIF-1-mediated pathway to improve disulfide bond formation and VEGF secretion under hypoxia: implication for cancer. Oncogene. 2005;24:1011-20 pubmed
  5. Zito E, Hansen H, Yeo G, Fujii J, Ron D. Endoplasmic reticulum thiol oxidase deficiency leads to ascorbic acid depletion and noncanonical scurvy in mice. Mol Cell. 2012;48:39-51 pubmed publisher
    ..Compromised ER disulfide relay thus exposes protein thiols to competing oxidation to sulfenic acid, resulting in depletion of ascorbic acid, impaired procollagen proline 4-hydroxylation, and a noncanonical form of scurvy. ..
  6. Qiang L, Wang H, Farmer S. Adiponectin secretion is regulated by SIRT1 and the endoplasmic reticulum oxidoreductase Ero1-L alpha. Mol Cell Biol. 2007;27:4698-707 pubmed
    ..These findings provide a framework to understand the mechanisms by which adipocytes regulate secretion of adiponectin in response to various metabolic states. ..
  7. Li G, Mongillo M, Chin K, Harding H, Ron D, Marks A, et al. Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol. 2009;186:783-92 pubmed publisher
    ..this response is blocked by siRNA-mediated silencing of ERO1-alpha or IP3R1 and by loss-of-function mutations in Ero1a or Chop. Reconstitution of ERO1-alpha in Chop(-/-) macrophages restores ER stress-induced IICR and apoptosis...
  8. Appenzeller Herzog C, Riemer J, Zito E, Chin K, Ron D, Spiess M, et al. Disulphide production by Ero1?-PDI relay is rapid and effectively regulated. EMBO J. 2010;29:3318-29 pubmed publisher
    ..Instead, our data suggest that a dynamic equilibrium between Ero1- and glutathione disulphide-mediated oxidation of PDIs constitutes an important element of ER redox homeostasis. ..
  9. Chin K, Kang G, Qu J, Gardner L, Coetzee W, Zito E, et al. The sarcoplasmic reticulum luminal thiol oxidase ERO1 regulates cardiomyocyte excitation-coupled calcium release and response to hemodynamic load. FASEB J. 2011;25:2583-91 pubmed publisher
    ..We established mouse lines with loss of function insertion mutations in Ero1l and Ero1lb encoding ERO1α and ERO1β...

More Information

Publications21

  1. Blais J, Chin K, Zito E, Zhang Y, Heldman N, Harding H, et al. A small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity. J Biol Chem. 2010;285:20993-1003 pubmed publisher
    b>Endoplasmic reticulum oxidation 1 (ERO1) is a conserved eukaryotic flavin adenine nucleotide-containing enzyme that promotes disulfide bond formation by accepting electrons from reduced protein disulfide isomerase (PDI) and passing them ..
  2. Zito E, Melo E, Yang Y, Wahlander Ã, Neubert T, Ron D. Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. Mol Cell. 2010;40:787-97 pubmed publisher
    ..These observations implicate ER-localized PRDX4 in a previously unanticipated, parallel, ERO1-independent pathway that couples hydroperoxide production to oxidative protein folding in mammalian cells. ..
  3. Kajiwara T, Tanaka T, Kukita K, Kutomi G, Saito K, Okuya K, et al. Hypoxia augments MHC class I antigen presentation via facilitation of ERO1-?-mediated oxidative folding in murine tumor cells. Eur J Immunol. 2016;46:2842-2851 pubmed publisher
  4. Grigaravicius P, Kaminska E, Hübner C, McKinnon P, von Deimling A, Frappart P. Rint1 inactivation triggers genomic instability, ER stress and autophagy inhibition in the brain. Cell Death Differ. 2016;23:454-68 pubmed publisher
    ..Altogether, our findings highlight the crucial roles of Rint1 in vivo in genomic stability maintenance, as well as in prevention of ER stress and autophagy. ..
  5. Wang Z, Schraw T, Kim J, Khan T, Rajala M, Follenzi A, et al. Secretion of the adipocyte-specific secretory protein adiponectin critically depends on thiol-mediated protein retention. Mol Cell Biol. 2007;27:3716-31 pubmed
    ..One mechanism for increasing circulating levels of specific adiponectin complexes by peroxisome proliferator-activated receptor gamma agonists may be selective upregulation of rate-limiting chaperones. ..
  6. Marino M, Stoilova T, Giorgi C, Bachi A, Cattaneo A, Auricchio A, et al. SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal muscle pathology, counteracts hyperoxidation by means of redox-regulating SERCA2 pump activity. Hum Mol Genet. 2015;24:1843-55 pubmed publisher
    ..These observations reveal the involvement of SEPN1 in ER redox and calcium homeostasis and that an ERO1 inhibitor, restoring redox-dependent calcium homeostasis, may ameliorate the myopathy of SEPN1 deficiency. ..
  7. Chen D, Jin K, Kawaguchi K, Nakayama M, Zhou X, Xiong Z, et al. Ero1-L, an ischemia-inducible gene from rat brain with homology to global ischemia-induced gene 11 (Giig11), is localized to neuronal dendrites by a dispersed identifier (ID) element-dependent mechanism. J Neurochem. 2003;85:670-9 pubmed
    ..Therefore, Ero-1L/Giig11 may have a role in ischemia-induced neuronal repair or survival mechanisms directed at counteracting abnormalities in protein folding, maturation and distribution. ..
  8. Avezov E, Cross B, Kaminski Schierle G, Winters M, Harding H, Melo E, et al. Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox. J Cell Biol. 2013;201:337-49 pubmed publisher
    ..These findings recommend fluorescent lifetime imaging as a sensitive method to track ER redox homeostasis in mammalian cells. ..
  9. Wright J, Birk J, Haataja L, Liu M, Ramming T, Weiss M, et al. Endoplasmic reticulum oxidoreductin-1? (Ero1?) improves folding and secretion of mutant proinsulin and limits mutant proinsulin-induced endoplasmic reticulum stress. J Biol Chem. 2013;288:31010-8 pubmed publisher
  10. Rao J, Zhang C, Wang P, Lu L, Qian X, Qin J, et al. C/EBP homologous protein (CHOP) contributes to hepatocyte death via the promotion of ERO1α signalling in acute liver failure. Biochem J. 2015;466:369-78 pubmed publisher
    ..Therefore, targeting CHOP/ERO1α signalling could be a novel therapeutic approach during ALF. ..
  11. Tanaka T, Kajiwara T, Torigoe T, Okamoto Y, Sato N, Tamura Y. Cancer-associated oxidoreductase ERO1-α drives the production of tumor-promoting myeloid-derived suppressor cells via oxidative protein folding. J Immunol. 2015;194:2004-10 pubmed publisher
    ..These results suggest that overexpression of ERO1-α in the tumor inhibits the T cell response by recruiting polymorphonuclear MDSCs via regulation of MDSC-prone cytokines and chemokines. ..
  12. Gess B, Hofbauer K, Wenger R, Lohaus C, Meyer H, Kurtz A. The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha. Eur J Biochem. 2003;270:2228-35 pubmed