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AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC

Author

Listed:
  • Veit Hornung

    (University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA
    Institute of Clinical Chemistry and Pharmacology)

  • Andrea Ablasser

    (University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA
    Institute of Clinical Chemistry and Pharmacology)

  • Marie Charrel-Dennis

    (University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA)

  • Franz Bauernfeind

    (University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA
    Institute of Clinical Chemistry and Pharmacology)

  • Gabor Horvath

    (University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA)

  • Daniel. R. Caffrey

    (Pfizer, 620 Memorial Drive, Cambridge, Massachusetts 02139, USA)

  • Eicke Latz

    (University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA)

  • Katherine A. Fitzgerald

    (University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA)

Abstract

Innate immunity sensor Cytoplasmic DNA is an important trigger for the innate immune system. The downstream signalling pathways involved in this process have been extensively characterized, but much less is known about the initial step, the recognition of the DNA. Two groups reporting in this issue of Nature have now identified AIM2 (absent in melanoma 2), a member of the interferon-inducible HIN-200 family, as a cytoplasmic DNA sensor. In the presence of DNA, AIM2 oligermerizes and associates with the adapter molecule ASC to activate NF-κB and caspase-1, key components of the inflammasome complex. This highlights the AIM2 inflammasome as a possible target for the treatment of both infections and autoimmune diseases.

Suggested Citation

  • Veit Hornung & Andrea Ablasser & Marie Charrel-Dennis & Franz Bauernfeind & Gabor Horvath & Daniel. R. Caffrey & Eicke Latz & Katherine A. Fitzgerald, 2009. "AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC," Nature, Nature, vol. 458(7237), pages 514-518, March.
    • Handle: RePEc:nat:nature:v:458:y:2009:i:7237:d:10.1038_nature07725
    DOI: 10.1038/nature07725
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    Cited by:

    1. Jonas D. Albarnaz & Joanne Kite & Marisa Oliveira & Hanqi Li & Ying Di & Maria H. Christensen & Joao A. Paulo & Robin Antrobus & Steven P. Gygi & Florian I. Schmidt & Edward L. Huttlin & Geoffrey L. S, 2023. "Quantitative proteomics defines mechanisms of antiviral defence and cell death during modified vaccinia Ankara infection," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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