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nature portfolio privacy policy gsdmd-egfp-expressing 293t-gsdmd-egfp cells model-building tools n-terminal his6-t7 tags dfna5-d270e-egfp-reconstituted 293t cells author information authors advertising ice-cold phosphate-buffered saline putative amphipathic nature 88-strand pore-forming β-barrel pan-caspase inhibitor zvad-fmk c-terminal-egfp tagged dfna5 c-terminal egfp-tagged dfna5 c-terminal egfp-tagged wt 293t-dfna5-d270e-egfp cells transfected pathogen-mediated inflammasome-suppression strategies44 social media 0/ reprints n-terminal moiety enriched mouse casp-1/casp-11-double knockout c-terminal his6 tags dfna5-d270e-egfp cell lines form anti-parallel β-hairpin 293t-dfna5-d270e-egfp cells dfna5-n-f2a-egfp mutant development stable 293t-gsdmd-egfp cells time-lapse confocal microscopy 293t-dfna5-egfp cells compared c-terminally truncated protein20 eucomm/komp-csd alleles exploratory research references wallach n-terminal sequence aahgi nature 514 nature 526 nature 535 nature 458 nature 474 nature receptor-interacting protein kinase-3 vsv-infected 293t-dfna5-egfp research reported specific pathogen-free conditions sds–polyacrylamide gel electrophoresis casp-1/11-deficient mice revealed author correspondence dnfa5 n-terminal helix death receptor-induced apoptotic

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         description:Apoptosis is a genetically regulated cell suicide programme mediated by activation of the effector caspases 3, 6 and 7. If apoptotic cells are not scavenged, they progress to a lytic and inflammatory phase called secondary necrosis. The mechanism by which this occurs is unknown. Here we show that caspase-3 cleaves the GSDMD-related protein DFNA5 after Asp270 to generate a necrotic DFNA5-N fragment that targets the plasma membrane to induce secondary necrosis/pyroptosis. Cells that express DFNA5 progress to secondary necrosis, when stimulated with apoptotic triggers such as etoposide or vesicular stomatitis virus infection, but disassemble into small apoptotic bodies when DFNA5 is deleted. Our findings identify DFNA5 as a central molecule that regulates apoptotic cell disassembly and progression to secondary necrosis, and provide a molecular mechanism for secondary necrosis. Because DFNA5-induced secondary necrosis and GSDMD-induced pyroptosis are dependent on caspase activation, we propose that they are forms of programmed necrosis. DFNA5 is related to the caspase-dependent pyroptosis inducer gasdermin D. Here the authors find that DFNA5 is cleaved by caspase 3 and show this cleavage skews cells away from apoptosis into secondary necrosis, a form of cell death characterized by membrane ballooning similar to pyroptosis.
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