ERO1-independent production of H2O2 within the endoplasmic reticulum fuels Prdx4-mediated oxidative protein folding

@inproceedings{Konno2015ERO1independentPO,
  title={ERO1-independent production of H2O2 within the endoplasmic reticulum fuels Prdx4-mediated oxidative protein folding},
  author={Tasuku Konno and Eduardo Pinho Melo and Carlos B. O. Lopes and Ilir Mehmeti and Sigurd Lenzen and David Ron and Edward Avezov},
  booktitle={The Journal of cell biology},
  year={2015}
}
The endoplasmic reticulum (ER)-localized peroxiredoxin 4 (PRDX4) supports disulfide bond formation in eukaryotic cells lacking endoplasmic reticulum oxidase 1 (ERO1). The source of peroxide that fuels PRDX4-mediated disulfide bond formation has remained a mystery, because ERO1 is believed to be a major producer of hydrogen peroxide (H2O2) in the ER lumen. We report on a simple kinetic technique to track H2O2 equilibration between cellular compartments, suggesting that the ER is relatively… CONTINUE READING
7 Citations
24 References
Similar Papers

References

Publications referenced by this paper.
Showing 1-10 of 24 references

A genetically encoded sensor for H 2 O 2 with expanded dynamic range

  • I. Mehmeti, S. Lortz
  • Bioorg . Med . Chem .
  • 2012

Ero 1 p : a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum

  • T. J. Tavender, N. J. Bulleid
  • Mol . Cell .
  • 2010

Similar Papers

Loading similar papers…