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Title:
ASC- and caspase-8-dependent apoptotic pathway diverges from the NLRC4 inflammasome in macrophages | Scientific Reports
Description:
The NLRC4 inflammasome recognizes bacterial flagellin and components of the type III secretion apparatus. NLRC4 stimulation leads to caspase-1 activation followed by a rapid lytic cell death known as pyroptosis. NLRC4 is linked to pathogen-free auto-inflammatory diseases, suggesting a role for NLRC4 in sterile inflammation. Here, we show that NLRC4 activates an alternative cell death program morphologically similar to apoptosis in caspase-1-deficient BMDMs. By performing an unbiased genome-wide CRISPR/Cas9 screen with subsequent validation studies in gene-targeted mice, we highlight a critical role for caspase-8 and ASC adaptor in an alternative apoptotic pathway downstream of NLRC4. Furthermore, caspase-1 catalytically dead knock-in (Casp1 C284A KI) BMDMs genetically segregate pyroptosis and apoptosis, and confirm that caspase-1 does not functionally compete with ASC for NLRC4 interactions. We show that NLRC4/caspase-8-mediated apoptotic cells eventually undergo plasma cell membrane damage in vitro, suggesting that this pathway can lead to secondary necrosis. Unexpectedly, we found that DFNA5/GSDME, a member of the pore-forming gasdermin family, is dispensable for the secondary necrosis that follows NLRC4-mediated apoptosis in macrophages. Together, our data confirm the existence of an alternative caspase-8 activation pathway diverging from the NLRC4 inflammasome in primary macrophages.
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caspase, cell, pubmed, death, article, nlrc, cells, bmdms, google, scholar, cas, asc, flagellin, activation, fig, caspcasp, nature, inflammasome, apoptosis, pyroptosis, dfna, macrophages, apoptotic, pathway, prestimulation, central, data, sgrna, ads, release, mice, membrane, secondary, alternative, necrosis, nlrcmediated, gsdmd, caspaseindependent, electroporation, caspasedependent, signaling, yoyo, httpsdoiorgnature, casp, plasma, conditions, pamcsk, ldh, absence, response,
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nature portfolio genome-wide crispr/cas9 screens privacy policy genome-wide crispr/cas9 screen genome-wide crispr-cas9 screen triple-deficient casp1−/−casp11−/−asc−/− bmdms advertising unbiased crispr/cas9 screen undergo asc/caspase-8-mediated apoptosis naip5/nlrc4-mediated cell death nlrc4/caspase-8-mediated cell death nlrc4-mas/scan4 patients develop academic libraries 48 tlr/nf-κb activation45 promote nf-κb signaling nlrc4-mediated caspase-1-dependent pyroptosis pathogen-free auto-inflammatory diseases fas/cd95-induced chemokines generated casp1−/−casp11−/−casp8−/−rip3k−/− mice stat-signaling activators ifn-α pathogen-induced cell death undergo caspase-8-mediated apoptosis caspase-8-dependent apoptotic pathway conserved carboxy-terminal domain casp1−/−casp11−/− cas9+ imac reprints caspase-1-independent cell death nlrc4-mediated cell death distinct dfna5-independent program caspase-8-mediated apoptosis pathway flagellin-induced cell death transcriptional anti-apoptotic program39 casp1−/−casp11−/− imacs proceeded interrogated casp1−/−casp11−/− imacs pore-forming gasdermin superfamily block caspase-8-dependent death caspase-1/gsdmd-dependent pyroptosis17 log2 fold-change greater nanoparticle-mediated cell pyroptosis nf-κb signaling tlr signaling-free conditions nf-kappab signals induce nlrc4/caspase-8-mediated apoptosis type-iii secretion system dfna5-independent secondary necrosis pore-forming gasdermin family nf-κb activators multi-protein inflammasome complexes caspase-3-induced secondary necrosis nlrc4-mas/scan4 focus
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headline:ASC- and caspase-8-dependent apoptotic pathway diverges from the NLRC4 inflammasome in macrophages
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headline:ASC- and caspase-8-dependent apoptotic pathway diverges from the NLRC4 inflammasome in macrophages
description:The NLRC4 inflammasome recognizes bacterial flagellin and components of the type III secretion apparatus. NLRC4 stimulation leads to caspase-1 activation followed by a rapid lytic cell death known as pyroptosis. NLRC4 is linked to pathogen-free auto-inflammatory diseases, suggesting a role for NLRC4 in sterile inflammation. Here, we show that NLRC4 activates an alternative cell death program morphologically similar to apoptosis in caspase-1-deficient BMDMs. By performing an unbiased genome-wide CRISPR/Cas9 screen with subsequent validation studies in gene-targeted mice, we highlight a critical role for caspase-8 and ASC adaptor in an alternative apoptotic pathway downstream of NLRC4. Furthermore, caspase-1 catalytically dead knock-in (Casp1 C284A KI) BMDMs genetically segregate pyroptosis and apoptosis, and confirm that caspase-1 does not functionally compete with ASC for NLRC4 interactions. We show that NLRC4/caspase-8-mediated apoptotic cells eventually undergo plasma cell membrane damage in vitro, suggesting that this pathway can lead to secondary necrosis. Unexpectedly, we found that DFNA5/GSDME, a member of the pore-forming gasdermin family, is dispensable for the secondary necrosis that follows NLRC4-mediated apoptosis in macrophages. Together, our data confirm the existence of an alternative caspase-8 activation pathway diverging from the NLRC4 inflammasome in primary macrophages.
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