From the Research
Inactivation of Activated AIM2 Inflammasome
To inactivate an activated Absent In Melanoma 2 (AIM2) inflammasome, several mechanisms can be considered based on the available research:
- Ubiquitination and proteasomal degradation: AIM2 is constitutively ubiquitinated and undergoes proteasomal degradation in resting cells to avoid autoinflammation 1. Enhancing this process could potentially inactivate the AIM2 inflammasome.
- Inhibition of USP21 deubiquitinase: USP21 deubiquitinates AIM2, increasing its protein stability and allowing for AIM2 inflammasome assembly 1. Inhibiting USP21 could prevent AIM2 inflammasome activation.
- Disruption of AIM2-ASC complex formation: The interaction between AIM2 and ASC is crucial for AIM2 inflammasome activation 2, 3, 4. Disrupting this interaction could inactivate the AIM2 inflammasome.
- Removal of cytoplasmic DNA: Since cytoplasmic DNA triggers AIM2 inflammasome activation 5, 2, 3, removing the DNA could potentially inactivate the inflammasome.
Key Components Involved in AIM2 Inflammasome Inactivation
The following components play a crucial role in AIM2 inflammasome activation and could be targeted for inactivation:
- AIM2: The cytoplasmic sensor that recognizes double-stranded DNA and assembles with ASC and caspase-1 to form the AIM2 inflammasome 5, 2, 3.
- ASC: The adaptor protein that interacts with AIM2 and caspase-1 to form the AIM2 inflammasome 2, 3, 4.
- USP21: The deubiquitinase that regulates AIM2 protein stability and AIM2 inflammasome assembly 1.