BCL-2 modulates the unfolded protein response by enhancing splicing of X-box binding protein-1.

@article{Chonghaile2015BCL2MT,
  title={BCL-2 modulates the unfolded protein response by enhancing splicing of X-box binding protein-1.},
  author={Tr{\'i}ona N{\'i} Chonghaile and Sanjeev M. Gupta and Mohan John and {\'E}va Szegezdi and Susan E Logue and Afshin Samali},
  journal={Biochemical and biophysical research communications},
  year={2015},
  volume={466 1},
  pages={40-5}
}
Accumulation of unfolded proteins within the endoplasmic reticulum (ER) triggers a highly conserved stress response mechanism termed the unfolded protein response (UPR). The UPR is a complex series of signaling pathways controlled by ER localized transmembrane receptors, PERK, ATF6 and IRE1α. Following activation IRE1α splices XBP-1 mRNA facilitating the formation of a potent transcription factor, spliced XBP-1. The BCL-2 family members, BAX and BAK, in addition to the mitochondrion also… CONTINUE READING
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