Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.

@article{Zito2010OxidativePF,
  title={Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin.},
  author={Ester Zito and Eduardo Pinho e Melo and Yun Yang and {\AA}sa Wahlander and Thomas A Neubert and David Ron},
  journal={Molecular cell},
  year={2010},
  volume={40 5},
  pages={787-97}
}
Endoplasmic reticulum (ER) oxidation 1 (ERO1) transfers disulfides to protein disulfide isomerase (PDI) and is essential for oxidative protein folding in simple eukaryotes such as yeast and worms. Surprisingly, ERO1-deficient mammalian cells exhibit only a modest delay in disulfide bond formation. To identify ERO1-independent pathways to disulfide bond formation, we purified PDI oxidants with a trapping mutant of PDI. Peroxiredoxin IV (PRDX4) stood out in this list, as the related cytosolic… CONTINUE READING