IRE1α induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress.

@article{Lerner2012IRE1IT,
  title={IRE1α induces thioredoxin-interacting protein to activate the NLRP3 inflammasome and promote programmed cell death under irremediable ER stress.},
  author={Alana G. Lerner and John-Paul Upton and Patil Praveen and Rajarshi Ghosh and Yoshimi Nakagawa and Aeid Igbaria and Sarah Shen and Vinh Ngoc Nguyen and Bradley J. Backes and Myriam Heiman and Nathaniel Heintz and Paul Greengard and Simon Hui and Qizhi Tang and Ala Trusina and Scott A. Oakes and Feroz R Papa},
  journal={Cell metabolism},
  year={2012},
  volume={16 2},
  pages={
          250-64
        }
}
When unfolded proteins accumulate to irremediably high levels within the endoplasmic reticulum (ER), intracellular signaling pathways called the unfolded protein response (UPR) become hyperactivated to cause programmed cell death. We discovered that thioredoxin-interacting protein (TXNIP) is a critical node in this "terminal UPR." TXNIP becomes rapidly induced by IRE1α, an ER bifunctional kinase/endoribonuclease (RNase). Hyperactivated IRE1α increases TXNIP mRNA stability by reducing levels of… CONTINUE READING
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