Caging NLRP3 tames inflammasome activity

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...

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Bibliographic Details
Published inCell Vol. 184; no. 26; pp. 6224 - 6226
Main Authors Schroder, Kate, Coll, Rebecca C
Format Journal Article
LanguageEnglish
Published United States 22.12.2021
Subjects
Cryoelectron Microscopy
Cytosol
Inflammasomes
NLR Family, Pyrin Domain-Containing 3 Protein
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Summary: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.
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ISSN:0092-8674
1097-4172
DOI:10.1016/j.cell.2021.11.035