Protein disulfide isomerase A6 controls the decay of IRE1α signaling via disulfide-dependent association.

@article{Eletto2014ProteinDI,
  title={Protein disulfide isomerase A6 controls the decay of IRE1α signaling via disulfide-dependent association.},
  author={Davide Eletto and Daniela Eletto and Devin Dersh and Tali Gidalevitz and Yair Argon},
  journal={Molecular cell},
  year={2014},
  volume={53 4},
  pages={562-576}
}
The response to endoplasmic reticulum (ER) stress relies on activation of unfolded protein response (UPR) sensors, and the outcome of the UPR depends on the duration and strength of signal. Here, we demonstrate a mechanism that attenuates the activity of the UPR sensor inositol-requiring enzyme 1α (IRE1α). A resident ER protein disulfide isomerase, PDIA6, limits the duration of IRE1α activity by direct binding to cysteine 148 in the lumenal domain of the sensor, which is oxidized when IRE1 is… CONTINUE READING
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