Cited by 143Inflammasome and immune disordersinterferon and immune responsesImmune Response and Inflammation

AIM2 inflammasome is activated by pharmacological disruption of nuclear envelope integrity

Open access
Di Micco, Antonia, Frera, Gianluca, Lugrin, Jérôme, Jamilloux, Yvan, Hsu, Erh-Ting, Tardivel, Aubry, De Gassart, Aude, Zaffalon, Léa +7 more·2016·Proceedings of the National Academy of Sciences

Abstract

Significance: Inflammasomes are cellular sensors of harmful situations such as the presence of microbes or alterations in cellular homeostasis. Upon activation, inflammasomes trigger the proteolytic maturation and release of inflammatory cytokines to initiate immune and repair responses. The assembly of inflammasome relies on a diverse repertoire of sensor proteins that can detect specific stimuli. For example, the AIM2 inflammasome is activated by the presence of microbial DNA within the cytosol. In this paper, alterations of the nuclear envelope integrity are found to cause the exposure of nuclear DNA in the cytosol to promote the activation of the AIM2 inflammasome. Nuclear envelope stress can therefore directly engage innate immune sensors to elicit inflammation.

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Crossref · 10.1073/pnas.1602419113

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  • CytoDNA species share similar signaling pathways, most prominently the cGAS-STING pathway, although mtDNA, MN, and other DNA damage-associated DNA fragments are thought to also activate the AIM2 and NLRP3 inflammasome pathway.

    “Third, cytoDNA species share similar signaling pathways, most prominently the cGAS-STING pathway, although mtDNA, MN, and other DNA damage-associated DNA fragments are thought to also activate the AIM2 and NLRP3 inflammasome pathway (Di Micco et al., 2016; Motwani and Fitzgerald, 2017; Zhong et al., 2018).”

    From Cytoplasmic DNA: sources, sensing, and role in aging and disease (2021) · cites this paper as Di Micco et al., 2016

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Authors
Di Micco, A., Frera, G., Lugrin, J., Jamilloux, Y., Hsu, E.-T., Tardivel, A., De Gassart, A., Zaffalon, L., Bujisic, B., Siegert, S., Quadroni, M., Broz, P., Henry, T., Hrycyna, C. A., & Martinon, F.
Affiliations
  • Department of Biochemistry, University of Lausanne, Epalinges 1066, Switzerland;
  • University of Lausanne (CH)
  • Inserm (FR)
  • Purdue University West Lafayette (US)
  • Focal Area Infection Biology, Biozentrum, University of Basel, 4056 Basel, Switzerland;
Venue
Proceedings of the National Academy of Sciences
Published
2016-07-26
Volume
113
Issue
32
Pages
E4671-80
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2477702703
Cited by
143
References
82
Citations by year
2026: 4 · 2025: 10 · 2024: 18 · 2023: 11 · 2022: 18 · 2021: 21 · 2020: 15 · 2019: 16 · 2018: 15 · 2017: 15
FWCI
7.97
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • IRIS (submittedVersion)
  • HAL (submittedVersion)
  • SERVAL (Université de Lausanne) (submittedVersion, other-oa)
Funders
EC | European Research Council (281996)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
  • Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords
AIM2 inflammasome, nelfinavir, nuclear envelope integrity, cytosolic DNA sensing, IL-1β, IL-1 signaling, HIV protease inhibitors, inflammasome activation
MeSH terms
NLR Family, Pyrin Domain-Containing 3 Protein, Animals, DNA, Mice, Inbred C57BL, Nuclear Envelope, Receptors, Interleukin-1, Nelfinavir, Caspase 1, Mice, CARD Signaling Adaptor Proteins, Interleukin-1beta, Inflammasomes

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