ArticleNature immunology2026
Cofilin-1 is a redox-sensitive guard of the NLRP3 inflammasome.
Article in Nature immunology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Theranostic peptide-selenium hydrogel targeting NETs-mitochondrial dysfunction-pyroptosis axis for chronic diabetic wound repair.Bioactive materials · 2027Article
- Metabolism, autophagy, and cell death: The triangular axis in tumor survival and therapeutic resistance.Redox biology · 2026Review
- ROS breaks the cofilin lock on NLRP3.Nature immunology · 2026Article
- Hypoxia-Induced Gut-Brain Axis Remodeling and Insomnia: Mechanisms and Microbiota Adaptive Regulation from a Translational Perspective.Journal of inflammation research · 2026Review
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Authors and funding
7 authors.
Funding
Abstract
Mutations in NLRP3 can cause a spectrum of the autoinflammatory cryopyrin-associated periodic syndromes (CAPS). Reactive oxygen species (ROS) have a central role in NLRP3 inflammasome activation. Here we show that cofilin-1, an actin-severing protein, is a negative regulator of the NLRP3 inflammasome. In resting cells, cofilin-1 directly bound NLRP3, but after stimulation with NLRP3 inflammasome activators, it was oxidized by ROS and dissociated from NLRP3. CAPS-associated mutant NLRP3 exhibited reduced binding to cofilin-1. Residues 101-104 of cofilin-1 were critical for NLRP3 interaction. Oxidation-independent peptides containing this NLRP3 binding motif suppressed inflammasome activation induced by endogenous CAPS-associated mutations and ex vivo NLRP3 activators such as ATP and nigericin. Bioinformatic structural analyses corroborate a model in which cofilin-1 has a pivotal function in NLRP3 activation by ROS and support the potential use of cofilin-1-derived peptides in individuals who are unresponsive to or intolerant of other forms of NLRP3 blockade.
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Registered trials
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