Figure 2.

Mitochondria serve as platforms for signalosome formation. The mitochondrial outer membrane is critical in activating the innate immune system by serving as the bridging platform for the aggregation of the MAVS protein and the formation of the NLRP3 inflammasome. Upon RNA virus infection, the protein TBK1 phosphorylates and inactivates the mitochondrial fission protein DRP1, critical for the fusion of mitochondria and the aggregation of MAVS for activation. Moreover, the mitochondrial outer membrane serves as a platform for the localization of TERRA-ZBP1 complexes formed under dysfunctional telomeres, leading to the activation of the MAVS pathway. Additionally, mitochondrial proteins such as cardiolipin, MAVS, and MFN2 have been shown to regulate the assembly of the NLRP3 inflammasome by providing binding sites for NLRP3.