MAVS is a critical mitochondrial adapter protein that orchestrates innate antiviral immunity by transducing signals from cytoplasmic RNA sensors RIG-I and MDA5 to activate type I interferon responses 1. Upon viral infection, MAVS undergoes phosphorylation by IKK and TBK1 kinases, enabling recruitment and activation of the transcription factor IRF3, which drives interferon-beta and other antiviral cytokine production 1. MAVS functions through multiple regulatory mechanisms: palmitoylation by ZDHHC24 enhances its aggregation and signaling capacity 2, while interaction with cellular mRNA 3' untranslated regions through its disordered domain organizes the MAVS signalosome complex 3. Conversely, lactate directly binds MAVS to suppress interferon production, linking metabolic state to immune activation 4. Beyond viral defense, MAVS participates in broader inflammatory contexts: it amplifies responses to unmodified circRNAs 5, drives senescence-associated inflammatory responses through mitochondrial dsRNA sensing 6, and mediates telomere dysfunction-induced tumor suppression 7. The asthma-susceptibility protein gasdermin B promotes MAVS-TBK1 signaling, contributing to respiratory inflammation 8. These findings establish MAVS as a central hub integrating metabolic, genetic, and stress signals to coordinate innate immunity.