Mitochondrial antiviral-signaling protein (MAVS) is a protein that in humans is encoded by the MAVSgene.[1][2][3] The protein is also known by the names VISA (virus-induced signaling adapter), IPS-1 and Cardif. Aggregated MAVS forms protease resistant prion-like aggregates that activate IRF3 dimerization.[4]
Function
Double-stranded RNA viruses are recognized in a cell type-dependent manner by the transmembrane receptor TLR3 or by the cytoplasmic RNA helicases MDA5 and RIG-I. These interactions initiate signalling pathways that differ in their initial steps but converge in the activation of the protein kinases IKKA (CHUK) and IKKB (IKBKB; MIM 603258), which activate NF-κB, or TBK1 and IKBKE, which activate IRF3. Activated IRF3 and NF-κB induce transcription of IFNβ (IFNB1). For the TLR3 pathway, the intermediary molecule before the pathways converge is the cytoplasmic protein TRIF (TICAM1). For RIG-I, the intermediary protein is mitochondria-bound MAVS.[3][5]
References
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↑Xu LG, Wang YY, Han KJ, Li LY, Zhai Z, Shu HB (Sep 2005). "VISA is an adapter protein required for virus-triggered IFN-beta signaling". Mol Cell. 19 (6): 727–40. doi:10.1016/j.molcel.2005.08.014. PMID16153868.
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Hirata Y, Broquet AH, Menchén L, Kagnoff MF (2007). "Activation of innate immune defense mechanisms by signaling through RIG-I/IPS-1 in intestinal epithelial cells". J. Immunol. 179 (8): 5425–32. doi:10.4049/jimmunol.179.8.5425. PMID17911629.
Liu S, Cai X, Wu J, Cong Q, Chen X, Li T, Du F, Ren J, Wu Y, Grishin N, Chen ZJ (2015). "Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation". Science. 347 (6227): aaa2630. doi:10.1126/science.aaa2630. PMID25636800.
