Caging NLRP3 tames inflammasome activity

Kate Schroder; Rebecca C Coll

doi:10.1016/j.cell.2021.11.035

Caging NLRP3 tames inflammasome activity

Cell. 2021 Dec 22;184(26):6224-6226. doi: 10.1016/j.cell.2021.11.035.

Authors

Kate Schroder¹, Rebecca C Coll²

Affiliations

¹ Institute for Molecular Bioscience and IMB Centre for Inflammation and Disease Research, The University of Queensland, St. Lucia, QLD 4072, Australia.
² The Wellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, Antrim, UK. Electronic address: r.coll@qub.ac.uk.

PMID: 34942097
DOI: 10.1016/j.cell.2021.11.035

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.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Cryoelectron Microscopy
Cytosol
Inflammasomes*
NLR Family, Pyrin Domain-Containing 3 Protein*

Substances

Inflammasomes
NLR Family, Pyrin Domain-Containing 3 Protein