IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response.

@article{Lee2002IRE1mediatedUM,
  title={IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response.},
  author={Kyungho Lee and Witoon Tirasophon and Xiaohua Shen and Marek Michalak and Ron Prywes and Tetsuya Okada and Hiderou Yoshida and Kazutoshi Mori and Randal J Kaufman},
  journal={Genes & development},
  year={2002},
  volume={16 4},
  pages={452-66}
}
All eukaryotic cells respond to the accumulation of unfolded proteins in the endoplasmic reticulum (ER) by signaling an adaptive pathway termed the unfolded protein response (UPR). In yeast, a type-I ER transmembrane protein kinase, Ire1p, is the proximal sensor of unfolded proteins in the ER lumen that initiates an unconventional splicing reaction on HAC1 mRNA. Hac1p is a transcription factor required for induction of UPR genes. In higher eukaryotic cells, the UPR also induces site-2 protease… CONTINUE READING
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