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

Seamus R. Morrone, Mariusz Matyszewski, Xiong Yu, Michael Delannoy, Edward H. Egelman and Jungsan Sohn ()
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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

Nature Communications, 2015, vol. 6, issue 1, 1-13

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms8827

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