Structural mechanisms in NLR inflammasome assembly and signaling

Zehan Hu, Jijie Chai

Research output: Chapter in Book/Report/Conference proceedingChapter

32 Scopus citations


Inflammasomes are multimeric protein complexes that mediate the activation of inflammatory caspases. One central component of inflammasomes is nucleotide-binding domain (NBD)-and leucine-rich repeat (LRR)-containing proteins (NLRs) that can function as pattern recognition receptors (PRRs). In resting cells, NLR proteins exist in an auto-inhibited, monomeric, and ADP-bound state. Perception of microbial or damage-associated signals results in NLR oligomerization, thus recruiting inflammatory caspases directly or through the adaptor molecule apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC). The assembled NLR inflammasomes serve as dedicated machinery to facilitate the activation of the inflammatory caspases. Here, we review current understanding of the structures of NLR inflammasomes with an emphasis on the molecular mechanisms of their assembly and activation. We also discuss implications of the self-propagation model derived from the NAIP-NLRC4 inflammasomes for the activation of other NLR inflammasomes and a potential role of the C-terminal LRR domain in the activation of an NLR protein.

Original languageEnglish (US)
Title of host publicationCurrent Topics in Microbiology and Immunology
PublisherSpringer Verlag
Number of pages20
StatePublished - Jul 1 2016
Externally publishedYes

Publication series

NameCurrent Topics in Microbiology and Immunology
ISSN (Print)0070-217X
ISSN (Electronic)2196-9965

ASJC Scopus subject areas

  • Immunology and Allergy
  • Microbiology
  • Immunology
  • Microbiology (medical)


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