Recombinant Human MAVS Protein Standard

Specifications

Form

Liquid

General info

Function

Adapter required for innate immune defense against viruses (PubMed : 16125763, PubMed : 16127453, PubMed : 16153868, PubMed : 16177806, PubMed : 19631370, PubMed : 20127681, PubMed : 20451243, PubMed : 21170385, PubMed : 23087404, PubMed : 27992402, PubMed : 33139700, PubMed : 37582970). 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 IFNB and RANTES (CCL5) (PubMed : 16125763, PubMed : 16127453, PubMed : 16153868, PubMed : 16177806, PubMed : 19631370, PubMed : 20127681, PubMed : 20451243, PubMed : 20628368, PubMed : 21170385, PubMed : 23087404, PubMed : 25636800, PubMed : 27736772, PubMed : 33110251). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state (PubMed : 20451243). 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 (PubMed : 20451243). May activate the same pathways following detection of extracellular dsRNA by TLR3 (PubMed : 16153868). May protect cells from apoptosis (PubMed : 16125763). Involved in NLRP3 inflammasome activation by mediating NLRP3 recruitment to mitochondria (PubMed : 23582325).

Post-translational modifications

Following activation, phosphorylated by TBK1 at Ser-442 in the pLxIS motif (PubMed:25636800, PubMed:27302953). 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 (PubMed:25636800).. Ubiquitinated (PubMed:19881509, PubMed:23087404, PubMed:25636800, PubMed:38016475). 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 (PubMed:19881509). Ubiquitinated by RNF125, leading to its degradation by the proteasome (PubMed:17460044). Undergoes 'Lys-48'-linked ubiquitination catalyzed by SMURF1 (PubMed:23087404). Ubiquitinated via 'Lys-63'-linked ubiquitination at Lys-10, Lys-311 and Lys-461 by UBE2N and TRIM31, promoting MAVS polymerization and formation of three-stranded helical filaments on mitochondria (PubMed:27992402, PubMed:37582970). Undergoes 'Lys-63'-linked ubiquitination leading to enhanced interaction between MAVS and TRAF2 (PubMed:34880843). Undergoes 'Lys-27'-linked ubiquitination by TRIM21 leading to enhanced interaction between MAVS and TBK1 (PubMed:29743353, PubMed:36943869). Deubiquitinated by USP10 leading to attenuation of RIGI-mediated MAVS aggregation and production of type I interferon (PubMed:37582970). Undergoes 'Lys-48'-linked polyubiquitination catalyzed by RNF115 leading to its degradation (PubMed:33139700).. Palmitoylated by ZHDDC4. Palmitoylation promotes MAVS stabilization and activation by inhibiting 'Lys-48'- but facilitating 'Lys-63'-linked ubiquitination.. Proteolytically cleaved by apoptotic caspases during apoptosis, leading to its inactivation (PubMed:30878284). Cleavage by CASP3 during virus-induced apoptosis inactivates it, preventing cytokine overproduction (PubMed:30878284).. (Microbial infection) Cleaved and degraded by hepatitis A virus (HAV) protein 3ABC allowing the virus to disrupt the activation of host IRF3 through the MDA5 pathway.. (Microbial infection) Cleaved by the protease 2A of coxsackievirus B3, poliovirus and enterovirus 71 allowing the virus to disrupt the host type I interferon production.. (Microbial infection) Cleaved by Seneca Valley virus protease 3C allowing the virus to suppress interferon type-I production.. (Microbial infection) Cleaved by HCV protease NS3/4A, thereby preventing the establishment of an antiviral state.. (Microbial infection) UFMylated by ULF1 in association with Epstein-Barr virus BILF1; leading to MAVS routing to the lysosome.

Subcellular localisation

Mitochondrion outer membrane