Increasing complexity of NLRP3 inflammasome regulation.

TitleIncreasing complexity of NLRP3 inflammasome regulation.
Publication TypeJournal Article
Year of Publication2020
AuthorsMoretti, J, J Blander, M
JournalJ Leukoc Biol
Date Published2020 Jun 12
ISSN1938-3673
Abstract

Inflammasomes are multiprotein complexes that assemble upon detection of danger signals to activate the inflammatory enzyme caspase-1, trigger secretion of the highly proinflammatory cytokine IL-1β, and induce an inflammatory cell death called pyroptosis. Distinctiveness of the nucleotide-binding oligomerization (NOD), Leucine-rich repeat (LRR)-containing protein (NLRP3) inflammasome resides in the diversity of molecules that induce its activation, indicating a certain intricacy. Furthermore, besides the canonical activation of NLRP3 in response to various stimuli, caspase-11-dependent detection of intracellular LPS activates NLRP3 through a noncanonical pathway. Several aspects of the NLRP3 inflammasome are not characterized or remain unclear. In this review, we summarize the different modes of NLRP3 activation. We describe recent insights into post-translational and cellular regulation that confer further complexity to NLRP3 inflammasomes.

DOI10.1002/JLB.3MR0520-104RR
Alternate JournalJ. Leukoc. Biol.
PubMed ID32531835
Grant ListDK072201 / GF / NIH HHS / United States
AI095245 / GF / NIH HHS / United States
AI123284 / GF / NIH HHS / United States