Molecular mechanisms of NLR proteins in inflammasome activation

Abstract

Nucleotide-binding domain and leucine-rich repeat-containing proteins (NLRs) are central mediators of inflammasome signaling, activating caspase-1 to drive pyroptotic cell death and pro-inflammatory responses. Although NLR activation is generally thought to involve conformational rearrangements that oligomerize their N- or C-terminal death domains to nucleate ASC or pro-caspase-1 oligomerization, the molecular mechanisms that enable these transitions vary substantially among family members. Here, we highlight recent structural advances that reveal how distinct NLRs are activated and assemble into higher-order signaling platforms, providing mechanistic insights into the diverse activation mechanisms that converge on a common inflammatory outcome.

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BibTeX RIS

BibTeX

@article{liu2026molecular,
  title = {{Molecular mechanisms of NLR proteins in inflammasome activation}},
  author = {Yichao Liu and Kexin Ji and Liman Zhang},
  journal = {Communications Biology},
  year = {2026},
  month = oct,
  doi = {10.1038/s42003-026-11169-w},
  url = {https://www.nature.com/articles/s42003-026-11169-w},
  note = {CC BY-NC-ND 4.0},
}

RIS

TY  - JOUR
TI  - Molecular mechanisms of NLR proteins in inflammasome activation
AU  - Yichao Liu
AU  - Kexin Ji
AU  - Liman Zhang
PY  - 2026
DA  - 2026/10/19
JO  - Communications Biology
DO  - 10.1038/s42003-026-11169-w
UR  - https://www.nature.com/articles/s42003-026-11169-w
AB  - Nucleotide-binding domain and leucine-rich repeat-containing proteins (NLRs) are central mediators of inflammasome signaling, activating caspase-1 to drive pyroptotic cell death and pro-inflammatory responses. Although NLR activation is generally thought to involve conformational rearrangements that oligomerize their N- or C-terminal death domains to nucleate ASC or pro-caspase-1 oligomerization, the molecular mechanisms that enable these transitions vary substantially among family members. Here, we highlight recent structural advances that reveal how distinct NLRs are activated and assemble into higher-order signaling platforms, providing mechanistic insights into the diverse activation mechanisms that converge on a common inflammatory outcome.
SN  - 2399-3642
ER  -

Abstract

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