ArticleNature communications2025
Clustering of NLRP3 induced by membrane or protein scaffolds promotes inflammasome assembly.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- P2X7-NEK7-NLRP3 Axis Drives Cardiac Inflammation and Fibrosis in Isoproterenol-Induced Cardiac Remodeling in Mice.Acta physiologica (Oxford, England) · 2026Article
- Phase separation drives NLRP3 inflammasome activation independently of Golgi localization.Cell death & disease · 2026Article
- Spatial control of NLRP3 inflammasome assembly by membrane lipid composition.Communications biology · 2026Review
- Stage-dependent role of NEK7 in the inactive-to-active conformational transition of NLRP3 monomer.PLoS computational biology · 2026Article
- Non-decameric NLRP3 reveals a TGN/MTOC-distal pathway of inflammasome activation.Nature communications · 2026Article
- Imidacloprid induces hepatorenal toxicity in male albino rats via oxidative, immune inflammatory, and proliferative effects: a 90-day study.Scientific reports · 2026Article
- Diverse Scaffolds Facilitate NLRP3 Clustering and Inflammasome Formation in Response to Perturbations in Cell Homeostasis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Post-translational modifications of NLRP3: to prime or not to prime?Trends in immunology · 2026Review
- NLRPs and tumor: research progress from molecular mechanisms to clinical applications.Oncogene · 2026Review
- An integrative computational approach for identification of NLRP3 inhibitors through machine learning, docking, dynamics and DFT analysis.Scientific reports · 2025Article
- Molecular mechanisms and regulation of inflammasome activation and signaling: sensing of pathogens and damage molecular patterns.Cellular & molecular immunology · 2025Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
NLRP3 is a pattern recognition receptor forming an inflammasome in response to diverse pathogen and self-derived triggers, but molecular insights on NLRP3 activation are still lacking. Here, we drive ectopic NLRP3 to different subcellular locations in NLRP3-deficient macrophages to map the spatial activation profile of NLRP3, and find that NLRP3 variants enriched at the organellar membranes respond to canonical triggers similarly to wild-type NLRP3; however, unlike wild-type, these NLRP3 variants can be activated even in the absence of the polybasic phospholipid-binding segment. Mechanistically, membrane or protein scaffolds mediate NLRP3 clustering, which leads to the unfastening of the inactive NACHT domain conformation preceding the activated NLRP3 oligomer formation. Our data thus suggest that scaffold-promoted clustering is an important step in NLRP3 activation, enabling NLRP3 to sense distinct activator-induced cellular anomalies exhibited via lipid or protein assemblies, thereby establishing NLRP3 as the master sensor of perturbations in cell homeostasis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.