RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL

@inproceedings{Lawlor2015RIPK3PC,
  title={RIPK3 promotes cell death and NLRP3 inflammasome activation in the absence of MLKL},
  author={Kate E Lawlor and Nufail Khan and Alison L Mildenhall and Motti Gerlic and Ben A Croker and Akshay A. D’Cruz and Cathrine M Hall and Sukhdeep Kaur Spall and H. Orsmond Anderton and Seth L Masters and Maryam Rashidi and Ian P Wicks and Warren S. Alexander and Yasuhiro Mitsuuchi and Christopher A. Benetatos and Stephen M. Condon and Wendy Wei-Lynn Wong and John Silke and David L. Vaux and James E Vince},
  booktitle={Nature communications},
  year={2015}
}
RIPK3 and its substrate MLKL are essential for necroptosis, a lytic cell death proposed to cause inflammation via the release of intracellular molecules. Whether and how RIPK3 might drive inflammation in a manner independent of MLKL and cell lysis remains unclear. Here we show that following LPS treatment, or LPS-induced necroptosis, the TLR adaptor protein TRIF and inhibitor of apoptosis proteins (IAPs: X-linked IAP, cellular IAP1 and IAP2) regulate RIPK3 and MLKL ubiquitylation. Hence, when… CONTINUE READING
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