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AIM2 Inflammasome Assembly and Signaling.

Bing Wang1, Yuan Tian2, Qian Yin3,4

  • 1Department of Biological Science, Florida State University, Tallahassee, FL, 32306, USA.

Advances in Experimental Medicine and Biology
|October 20, 2019
PubMed
Summary

The AIM2 inflammasome senses double-stranded DNA, initiating inflammatory responses. Structural studies reveal how AIM2, ASC, and caspase-1 assemble into filaments, providing insights into inflammasome activation and regulation.

Keywords:
AIM2ASCCARDCOPCaspase-1HINHelical filamentInflammasomePOPPYDp202

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Area of Science:

  • Molecular Biology
  • Immunology
  • Structural Biology

Background:

  • AIM2 (absent in melanoma 2) is a key cytoplasmic sensor for double-stranded DNA (dsDNA).
  • It triggers the AIM2 inflammasome, leading to caspase-1 activation, cytokine maturation, and pyroptosis.
  • Understanding AIM2 inflammasome assembly is crucial for deciphering innate immune responses.

Purpose of the Study:

  • To elucidate the structural mechanisms of AIM2 inflammasome activation and assembly.
  • To detail the interactions between dsDNA, AIM2, ASC, and caspase-1.
  • To highlight the role of helical filament formation in PYD and CARD domains.

Main Methods:

  • X-ray crystallography
  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Cryo-electron microscopy (cryo-EM)

Main Results:

  • Detailed structural insights into AIM2 inflammasome components and their interactions.
  • Characterization of helical filament assembly involving PYD and CARD domains.
  • Understanding the regulation of AIM2 inflammasome activation.

Conclusions:

  • Structural studies provide a comprehensive view of AIM2 inflammasome assembly and activation.
  • The principles governing AIM2 inflammasome assembly are applicable to other inflammasome systems.
  • This work deepens our understanding of innate immunity and inflammatory signaling pathways.