The NLRP3 inflammasome: activation and regulation |
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| Institution: | 1. Department of Synthetic Biology and Immunology, National Institute of Chemistry, Hajdrihova 19, Ljubljana, 1000, Slovenia;2. EN-FIST Centre of Excellence, Trg Osvobodilne Fronte 13, Ljubljana, Slovenia;1. VCU Pauley Heart Center, Division of Cardiology, Department of Internal Medicine, Virginia Commonwealth University, Richmond, VA, USA;2. Department of Pharmacotherapy and Outcome Studies, Virginia Commonwealth University, Richmond, VA, USA;3. Department of Pharmacy, Brigham and Women''s Hospital, Boston, MA, USA;4. Department of Innovative Technologies in Medicine and Dentistry, “G. d''Annunzio” University of Chieti-Pescara, Chieti, Italy;5. Department of Medicine and Ageing Sciences, “G. d''Annunzio” University of Chieti-Pescara, Chieti, Italy;6. Department of Medical-Surgical Sciences and Biotechnologies, Sapienza University of Rome, Latina, Italy;7. Mediterranea Cardiocentro, Napoli, Italy;8. Wright Center for Clinical and Translational Research, Virginia Commonwealth University, Richmond, VA, USA;1. Department of Immunology, St. Jude Children''s Research Hospital, Memphis, TN 38105, USA |
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| Abstract: | The NOD-, LRR- and pyrin domain-containing protein 3 (NLRP3) inflammasome is a cytoplasmic supramolecular complex that is activated in response to cellular perturbations triggered by infection and sterile injury. Assembly of the NLRP3 inflammasome leads to activation of caspase-1, which induces the maturation and release of interleukin-1β (IL-1β) and IL-18, as well as cleavage of gasdermin D (GSDMD), which promotes a lytic form of cell death. Production of IL-1β via NLRP3 can contribute to the pathogenesis of inflammatory disease, whereas aberrant IL-1β secretion through inherited NLRP3 mutations causes autoinflammatory disorders. In this review, we discuss recent developments in the structure of the NLRP3 inflammasome, and the cellular processes and signaling events controlling its assembly and activation. |
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