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Mitochondrial antiviral-signaling protein

Mitochondrial antiviral-signaling protein (MAVS) is a protein that in humans is encoded by the MAVS gene.[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

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

References

  1. Seth RB, Sun L, Ea CK, Chen ZJ (Sep 2005). “Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3”. Cell. 122 (5): 669–82. doi:10.1016/j.cell.2005.08.012. PMID 16125763.
  2. 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. PMID 16153868.
  3. 3.0 3.1 “Entrez Gene: VISA virus-induced signaling adapter”.
  4. Hou F, Sun L, Zheng H, Skaug B, Jiang QX, Chen ZJ (Aug 5, 2011). “MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response”. Cell. 146 (3): 448–61. doi:10.1016/j.cell.2011.06.041. PMC 3179916. PMID 21782231.
  5. Sen GC, Sarkar SN (2005). “Hitching RIG to action”. Nat. Immunol. 6 (11): 1074–6. doi:10.1038/ni1105-1074. PMID 16239922.
Further reading

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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