Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes
Open accessAbstract
Inflammasomes elicit host defense inside cells by activating caspase-1 for cytokine maturation and cell death. AIM2 and NLRP3 are representative sensor proteins in two major families of inflammasomes. The adaptor protein ASC bridges the sensor proteins and caspase-1 to form ternary inflammasome complexes, achieved through pyrin domain (PYD) interactions between sensors and ASC and through caspase activation and recruitment domain (CARD) interactions between ASC and caspase-1. We found that PYD and CARD both form filaments. Activated AIM2 and NLRP3 nucleate PYD filaments of ASC, which, in turn, cluster the CARD of ASC. ASC thus nucleates CARD filaments of caspase-1, leading to proximity-induced activation. Endogenous NLRP3 inflammasome is also filamentous. The cryoelectron microscopy structure of ASC(PYD) filament at near-atomic resolution provides a template for homo- and hetero-PYD/PYD associations, as confirmed by structure-guided mutagenesis. We propose that ASC-dependent inflammasomes in both families share a unified assembly mechanism that involves two successive steps of nucleation-induced polymerization. PAPERFLICK:
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Pro-caspase-1 undergoes proximity-induced autoproteolysis, leading to active caspase-1 processing pro-IL-1β and pro-IL-18 into their mature forms and subsequent secretion.
“Pro-caspase-1 then undergoes proximity-induced autoproteolysis, which leads to active caspase-1 processing pro-IL-1β and pro-IL-18 into their mature forms IL-1β and IL-18 and the subsequent secretion of these cytokines [55, 58, 61–63]”
From Microglial function, INPP5D/SHIP1 signaling, and NLRP3 inflammasome activation: implications for Alzheimer’s disease (2023) · cites this paper as [61]
The Discussion (page unavailable) proposes that caspase-1 dimerization within inflammasome filaments may cause intradimer cleavage and enhance enzymatic activity; it does not establish autoproteolysis as a definite step. The Results report caspase-1 processing pro-IL-1β into mature IL-1β, and the Introduction links caspase activation to IL-18 maturation. Our copy does not state that the mature cytokines are subsequently secreted. (LLM, conf=0.86)
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- Authors
- Lu, A., Magupalli, V. G., Ruan, J., Yin, Q., Atianand, M. K., Vos, M. R., Schröder, G. F., Fitzgerald, K. A., Wu, H., & Egelman, E. H.
- Affiliations
- Boston Children's Hospital (US)
- University of Massachusetts Chan Medical School (US)
- University of Virginia (US)
- Corresponding author
- Wu, Hao
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2014-03
- Volume
- 156
- Issue
- 6
- Pages
- 1193-1206
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC4000066
- OpenAlex
- W2078850432
- Cited by
- 1,353
- References
- 3
- Citations by year
- 2026: 103 · 2025: 114 · 2024: 128 · 2023: 133 · 2022: 149 · 2021: 110 · 2020: 130 · 2019: 111 · 2018: 90 · 2017: 83 · 2016: 74 · 2015: 79 · 2014: 45 · 2012: 1
- FWCI
- 38.43
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship@UMassChan (submittedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (AI050872, R01AI050872, AI083713, R01AI083713)
- National Institute of Biomedical Imaging and Bioengineering (R01EB001567, EB 001567)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Keywords
- ASC, inflammasome assembly, AIM2, NLRP3, caspase-1, pyrin domain, CARD domain, filament nucleation, polymerization, cryo-EM structure
- MeSH terms
- NLR Family, Pyrin Domain-Containing 3 Protein, Amino Acid Sequence, Carrier Proteins, Cytoskeletal Proteins, DNA-Binding Proteins, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Protein Structure, Tertiary, Cryoelectron Microscopy, CARD Signaling Adaptor Proteins, Interleukin-1beta, Polymerization, Inflammasomes
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