On the mechanism of sensing unfolded protein in the endoplasmic reticulum.

@article{Credle2005OnTM,
  title={On the mechanism of sensing unfolded protein in the endoplasmic reticulum.},
  author={Joel J. Credle and Janet S Finer-Moore and Feroz R Papa and Robert Michael Stroud and Peter Walter},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 52},
  pages={
          18773-84
        }
}
Unfolded proteins in the endoplasmic reticulum (ER) activate the ER transmembrane sensor Ire1 to trigger the unfolded protein response (UPR), a homeostatic signaling pathway that adjusts ER protein folding capacity according to need. Ire1 is a bifunctional enzyme, containing cytoplasmic kinase and RNase domains whose roles in signal transduction downstream of Ire1 are understood in some detail. By contrast, the question of how its ER-luminal domain (LD) senses unfolded proteins has remained an… CONTINUE READING

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