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Assembly-driven activation of the AIM2 foreign-dsDNA sensor provides a polymerization template for downstream ASC

Author

Listed:
  • Seamus R. Morrone

    (Johns Hopkins University School of Medicine)

  • Mariusz Matyszewski

    (Johns Hopkins University School of Medicine)

  • Xiong Yu

    (University of Virginia School of Medicine)

  • Michael Delannoy

    (Microscope Core Facilities, Johns Hopkins University School of Medicine)

  • Edward H. Egelman

    (University of Virginia School of Medicine)

  • Jungsan Sohn

    (Johns Hopkins University School of Medicine)

Abstract

AIM2 recognizes foreign dsDNA and assembles into the inflammasome, a filamentous supramolecular signalling platform required to launch innate immune responses. We show here that the pyrin domain of AIM2 (AIM2PYD) drives both filament formation and dsDNA binding. In addition, the dsDNA-binding domain of AIM2 also oligomerizes and assists in filament formation. The ability to oligomerize is critical for binding dsDNA, and in turn permits the size of dsDNA to regulate the assembly of the AIM2 polymers. The AIM2PYD oligomers define the filamentous structure, and the helical symmetry of the AIM2PYD filament is consistent with the filament assembled by the PYD of the downstream adaptor ASC. Our results suggest that the role of AIM2PYD is not autoinhibitory, but generating a structural template by coupling ligand binding and oligomerization is a key signal transduction mechanism in the AIM2 inflammasome.

Suggested Citation

  • Seamus R. Morrone & Mariusz Matyszewski & Xiong Yu & Michael Delannoy & Edward H. Egelman & Jungsan Sohn, 2015. "Assembly-driven activation of the AIM2 foreign-dsDNA sensor provides a polymerization template for downstream ASC," Nature Communications, Nature, vol. 6(1), pages 1-13, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8827
    DOI: 10.1038/ncomms8827
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    Cited by:

    1. Meenakshi Sharma & Eva Alba, 2023. "Assembly mechanism of the inflammasome sensor AIM2 revealed by single molecule analysis," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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