Homeostatic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity

@inproceedings{Rubio2011HomeostaticAT,
  title={Homeostatic adaptation to endoplasmic reticulum stress depends on Ire1 kinase activity},
  author={Claudia A. Rubio and David Pincus and Alexei V. Korennykh and Sebastian Schuck and Hana El-Samad and Peter J. Walter},
  booktitle={The Journal of cell biology},
  year={2011}
}
Accumulation of misfolded proteins in the lumen of the endoplasmic reticulum (ER) activates the unfolded protein response (UPR). Ire1, an ER-resident transmembrane kinase/RNase, senses the protein folding status inside the ER. When activated, Ire1 oligomerizes and trans-autophosphorylates, activating its RNase and initiating a nonconventional mRNA splicing reaction. Splicing results in production of the transcription factor Hac1 that induces UPR target genes; expression of these genes restores… CONTINUE READING
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