A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells.

@article{AppenzellerHerzog2008AND,
  title={A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells.},
  author={Christian Appenzeller-Herzog and Jan Riemer and Brian Christensen and Esben Skipper S\orensen and Lars Ellgaard},
  journal={The EMBO journal},
  year={2008},
  volume={27 22},
  pages={2977-87}
}
Oxidative maturation of secretory and membrane proteins in the endoplasmic reticulum (ER) is powered by Ero1 oxidases. To prevent cellular hyperoxidation, Ero1 activity can be regulated by intramolecular disulphide switches. Here, we determine the redox-driven shutdown mechanism of Ero1alpha, the housekeeping Ero1 enzyme in human cells. We show that functional silencing of Ero1alpha in cells arises from the formation of a disulphide bond-identified by mass spectrometry--between the active-site… CONTINUE READING
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