Structural basis for the oligomerization-mediated regulation of NLRP3 . . . A multilayered regulatory mechanism ensures proper NLRP3 inflammasome activation, although the structural basis for this process remains unclear This study aimed to investigate the cryo-electron microscopy structure of the dodecameric form of full-length NLRP3 bound to the clinically relevant NLRP3-specific inhibitor MCC950
A single amino acid residue defines the difference in NLRP3 . . . Here, we show that the mouse NEK7 catalytic domain, which shares high sequence identity with the counterpart of NEK6, mediates its interaction with NLRP3 and inflammasome activation in mouse macrophages
The NLRP3 Inflammasome: Mechanisms of Activation, Regulation, and . . . In this review, we provide an updated overview of the molecular mechanisms governing NLRP3 activation and regulation, with particular focus on ion flux, mitochondrial damage, lysosomal rupture, reactive oxygen species, and post-translational modifications
NLRP3 Phospho-residue Mapping by Phospho Dot Blots NLRP3 (the NOD, LRR, and pyrin domain-containing protein 3), which initiates the formation of an NLRP3 inflammasome complex, is regulated posttranslationally by phosphorylation at several Ser and Tyr residues However, determining sites of modification are not straightforward
A detailed molecular network map and model of the NLRP3 inflammasome We present a detailed reconstruction of the molecular network surrounding the NLRP3 inflammasome, which account for each specific reaction and the known regulatory constraints on each event as well as the mechanisms of drug action and impact of genetics when known
Cryo-EM structures of the active NLRP3 inflammasome disc Here we report cryogenic electron microscopy structures of disc-shaped active NLRP3 oligomers in complex with adenosine 5′-O- (3-thio)triphosphate, the centrosomal NIMA-related kinase 7 (NEK7)
Consecutive palmitoylation and phosphorylation orchestrates NLRP3 . . . These findings unveil a mechanism of consecutive palmitoylation and phosphorylation events in fine-tuning NLRP3 subcellular trafficking and activation, with implications for potential therapies for NLRP3-dysregulation-associated inflammatory diseases
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