Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum.

@article{Molteni2004GlutathioneLE,
  title={Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum.},
  author={Silvia Nerini Molteni and Anna Fassio and Maria Rosa Ciriolo and Giuseppe Filomeni and Elena Pasqualetto and Claudio Fagioli and Roberto Sitia},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 31},
  pages={32667-73}
}
Many proteins of the secretory pathway contain disulfide bonds that are essential for structure and function. In the endoplasmic reticulum (ER), Ero1 alpha and Ero1 beta oxidize protein disulfide isomerase (PDI), which in turn transfers oxidative equivalents to newly synthesized cargo proteins. However, oxidation must be limited, as some reduced PDI is necessary for disulfide isomerization and ER-associated degradation. Here we show that in semipermeable cells, PDI is more oxidized, disulfide… CONTINUE READING

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