Caging NLRP3 tames inflammasome activity
- PMID: 34942097
- DOI: 10.1016/j.cell.2021.11.035
Caging NLRP3 tames inflammasome activity
Abstract
How the danger sensor NLRP3 is activated is intensively debated. Using cryo-electron microscopy (EM) approaches, Andreeva and colleagues made the remarkable discovery that inactive NLRP3 forms a double ring of 12-16 monomers that shield its pyrin domains from the cytosol. We discuss this surprising new mechanism of inflammasome regulation.
Copyright © 2021 Elsevier Inc. All rights reserved.
Conflict of interest statement
Declaration of interests K.S. and R.C.C. are co-inventors on patent applications for NLRP3 inhibitors which have been licensed to Inflazome Ltd. K.S. served on the Scientific Advisory Board of Inflazome in 2016–2017 and is a consultant for Quench Bio and Novartis. R.C.C. is a consultant for BioAge Labs.
Comment on
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NLRP3 cages revealed by full-length mouse NLRP3 structure control pathway activation.Cell. 2021 Dec 22;184(26):6299-6312.e22. doi: 10.1016/j.cell.2021.11.011. Epub 2021 Dec 2. Cell. 2021. PMID: 34861190 Free PMC article.
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