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10.1016/j.celrep.2016.05.032

http://scihub22266oqcxt.onion/10.1016/j.celrep.2016.05.032
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C4909532!4909532!27264187
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suck abstract from ncbi


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pmid27264187      Cell+Rep 2016 ; 15 (11): 2449-61
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  • CYLD proteolysis protects macrophages from TNF-mediated auto-necroptosis induced by LPS and licensed by type I IFN #MMPMID27264187
  • Legarda D; Justus SJ; Ang RL; Rikhi N; Li W; Moran TM; Zhang J; Mizoguchi E; Zelic M; Kelliher MA; Blander JM; Ting AT
  • Cell Rep 2016[Jun]; 15 (11): 2449-61 PMID27264187show ga
  • Tumor necrosis factor (TNF) induces necroptosis, a RIPK3/MLKL-dependent form of inflammatory cell death. In response to infection by Gram-negative bacteria, multiple receptors on macrophages including TLR4, TNF and type I IFN receptors are concurrently activated but it is unclear how they crosstalk to regulate necroptosis. We report that TLR4 activates CASPASE-8 to cleave and remove the deubiquitinase CYLD in a TRIF- and RIPK1-dependent manner to disable necroptosis in macrophages. Inhibiting CASPASE-8 leads to CYLD-dependent necroptosis caused by the TNF produced in response to TLR4 ligation. While LPS-induced necroptosis was abrogated in Tnf?/? macrophages, a soluble TNF antagonist was not able to do so in Tnf+/+ macrophages, indicating that necroptosis occurs in a cell-autonomous manner. Surprisingly, TNF-mediated auto-necroptosis of macrophages requires type I IFN, which primes the expression of key necroptosis-signaling molecules including TNFR2 and MLKL. Thus, the TNF necroptosis pathway is regulated by both negative and positive crosstalk.
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