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- W4280496322 abstract "Inflammasomes sense intrinsic and extrinsic danger signals to trigger inflammatory responses and pyroptotic cell death. Homotypic pyrin domain (PYD) interactions of inflammasome forming nucleotide-binding oligomerization domain (NOD)–like receptors with the adaptor protein ASC (apoptosis-associated speck-like protein containing a CARD) mediate oligomerization into filamentous assemblies. We describe the cryo–electron microscopy (cryo-EM) structure of the human NLRP3 PYD filament and identify a pattern of highly polar interface residues that form the homomeric interactions leading to characteristic filament ends designated as A- and B-ends. Coupling a titration polymerization assay to cryo-EM, we demonstrate that ASC adaptor protein elongation on NLRP3 PYD nucleation seeds is unidirectional, associating exclusively to the B-end of the filament. Notably, NLRP3 and ASC PYD filaments exhibit the same symmetry in rotation and axial rise per subunit, allowing a continuous transition between NLRP3 and ASC. Integrating the directionality of filament growth, we present a molecular model of the ASC speck consisting of active NLRP3, ASC, and Caspase-1 proteins." @default.
- W4280496322 created "2022-05-22" @default.
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- W4280496322 date "2022-05-13" @default.
- W4280496322 modified "2023-10-18" @default.
- W4280496322 title "Directionality of PYD filament growth determined by the transition of NLRP3 nucleation seeds to ASC elongation" @default.
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- W4280496322 doi "https://doi.org/10.1126/sciadv.abn7583" @default.
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- W4280496322 hasPublicationYear "2022" @default.
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