Both CARD and transmembrane domains are essential for antiviral function. The CARD domain is responsible for interaction with RIGI and IFIH1/MDA5 (By similarity).
The transmembrane domain and residues 285-420 are essential for its interaction with DHX58/LGP2.
The pLxIS motif constitutes an IRF3-binding motif: following phosphorylation by TBK1, the phosphorylated pLxIS motif of MAVS recruits IRF3. IRF3 is then phosphorylated and activated by TBK1 to induce type-I interferons and other cytokines.
Both CARD and transmembrane domains are essential for antiviral function. The CARD domain is responsible for interaction with RIGI and IFIH1/MDA5.
The transmembrane domain and residues 300-444 are essential for its interaction with DHX58/LGP2.
Adapter required for innate immune defense against viruses (PubMed:24037184). Acts downstream of DHX33, RIGI and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFN-beta and RANTES (CCL5) (PubMed:24037184). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state (By similarity). Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response (By similarity). May activate the same pathways following detection of extracellular dsRNA by TLR3 (By similarity). May protect cells from apoptosis (By similarity). Involved in NLRP3 inflammasome activation by mediating NLRP3 recruitment to mitochondria (PubMed:23582325).
Following activation, phosphorylated by TBK1 at Ser-418 in the pLxIS motif. The phosphorylated pLxIS motif constitutes an IRF3-binding motif, leading to recruitment of the transcription factor IRF3 to induce type-I interferons and other cytokines.
Ubiquitinated. Undergoes 'Lys-48'-linked polyubiquitination catalyzed by ITCH; ITCH-dependent polyubiquitination is mediated by the interaction with PCBP2 and leads to MAVS/IPS1 proteasomal degradation. Ubiquitinated by RNF125, leading to its degradation by the proteasome. Undergoes 'Lys-48'-linked ubiquitination catalyzed by SMURF1. Ubiquitinated via 'Lys-63'-linked ubiquitination at Lys-10 by TRIM31, promoting MAVS polymerization and formation of three-stranded helical filaments on mitochondria. Undergoes 'Lys-63'-linked ubiquitination leading to enhanced interaction between MAVS and TRAF2. Undergoes 'Lys-27'-linked ubiquitination by UBE2N and TRIM21 leading to enhanced interaction between MAVS and TBK1 (By similarity). Deubiquitinated by USP10 leading to attenuation of RIGI-mediated MAVS aggregation and production of type I interferon (By similarity). Undergoes 'Lys-48'-linked polyubiquitination catalyzed by RNF115 leading to its degradation (By similarity).
Proteolytically cleaved by apoptotic caspases during apoptosis, leading to its inactivation. Cleavage by CASP3 during virus-induced apoptosis inactivates it, preventing cytokine overproduction.
Palmitoylated by ZHDDC4. Palmitoylation promotes MAVS stabilization and activation by inhibiting 'Lys-48'- but facilitating 'Lys-63'-linked ubiquitination.
Proteins
53399Da
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