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• W3001103407 abstract "SUMMARY Caspase-4 directly senses and is activated by cytosolic LPS in conditions of pathogen infection. It is unclear whether and how caspase-4 detects host derived factors for triggering pyroptosis. Here we show that mitochondrial permeability transition (MPT) promotes the assembly of a protein complex comprised of Apaf-1 and caspase-4 (caspase-11 in mice), defined herein as pyroptosome, for the execution of facilitated pyroptosis. MPT induced by bile acids and calcium overload, and specifically by an adenine nucleotide translocator 1 (ANT1) activator, triggered pyroptosome assembly. Different from the direct cleavage of GSDMD by LPS-activated caspase-4, caspase-4 activated in the Apaf-1 pyroptosome proceeds to cleave caspase-3 and thereby gasdermin E (GSDME) to induce pyroptosis. Caspase-11 initiated and GSDME executed pyroptosis underlies cholesteric liver failure. These findings identify Apaf-1 pyroptosome as a pivotal machinery for cells sensing MPT signals and may shed lights on understanding how cells execute pyroptosis under sterile conditions. Highlights Bile acids trigger caspase-4/11 and GSDME dependent pyroptosis Caspase-4/11 is a general sensor of mitochondrial permeability transition (MPT) MPT drives Apaf-1/capase-4 pryoptosome assembly Caspase-11 and GSDME mediated pyroptosis underlies cholesteric liver damage eTOC Blurb Persistent mitochondrial permeability transition elicited by bile acids, calcium overload and specifically ANT1 activators drives assembly of Apaf-1-capase-4/11 pyroptosome triggering GSDME dependent pryroptosis." @default.
• W3001103407 created "2020-01-30" @default.
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• W3001103407 date "2020-01-27" @default.
• W3001103407 modified "2023-09-23" @default.
• W3001103407 title "Apaf-1 Pyroptosome Senses Mitochondrial Permeability Transition" @default.
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• W3001103407 doi "https://doi.org/10.1101/2020.01.27.921122" @default.
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