Ontology highlight
ABSTRACT:
SUBMITTER: Morrone SR
PROVIDER: S-EPMC4525163 | biostudies-literature | 2015 Jul
REPOSITORIES: biostudies-literature
Nature communications 20150722
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 (AIM2(PYD)) 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 pol ...[more]