|Homo sapiens Gene: MAVS
|2014-10-13 [Report errors or provide feedback]
|mitochondrial antiviral signaling protein
mitochondrial antiviral signaling protein
mitochondrial antiviral signaling protein
|Stemformatics EHFPI ImmGen
MAVS oligomer is essential in the formation of a multiprotein membrane-associated signalling complex that enables downstream activation of IRF3 and NF-kappaB in antiviral innate immunity.
MAVS is a caspase recruitment domain (CARD)-containing adaptor protein that interacts with DDX58 (RIG-I) and recruits CHUK (IKKalpha), IKBKB (IKKbeta) and IKBKE (IKKepsilon) kinases by means of its C-terminal region, leading to the activation of NF-kappaB and IRF3.
MAVS is an adaptor protein that contains an N-terminal caspase recruitment domain (CARD)-like domain and a C-terminal transmembrane domain, both of which are essential for MAVS signalling, while the transmembrane domain also targets MAVS to the mitochondria.
MAVS facilitates cell death by disrupting the mitochondrial membrane potential and by activating caspases.
MAVS-dependent RIG-I-like receptor (RLR) signalling regulates the quantity, quality, and balance of the immune response to West Nile virus (WNV) infection.
MAVS in peroxisomes induces a rapid interferon-independent expression of defence factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signalling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response.
MAVS interacts with hepatitis B virus X protein and this promotes the degradation of MAVS via Lys(136) ubiquitination, preventing the induction of IFN-beta.
MAVS (IPS-1) interacts with MFN1 upon virus-infection or 5'ppp-RNA activation through redistribution of MAVS to form speck-like aggregates in cells.
MAVS (IPS1) plays an important role in regulating the host anti-viral response by binding to viral polymerase and inhibiting IFN-beta production.
MAVS negatively regulates the stability of voltage-dependent anion channel 1 (VDAC1) and thereby inhibits apoptosis in the response to release of cytochrome c.
The MAVS signalling pathway in non-myeloid cells is crucial for dsRNA-mediated natural killer cell activation. (Demonstrated in murine model)
Tyrosine phosphorylation of MAVS at amino acid residue Tyr9 is critical for the induction of IFNB signalling.
MAVS mRNA is degraded in response to foreign RNA and poly(I:C) to suppress hyper-immune reaction in late-phase antiviral signalling.
MAVS is required for optimal NLRP3 inflammasome activity by mediating mitochondrial recruitment of NLRP3.
MAVS is targeted by enterovirus protease to evade antiviral immunity.
The binding of MAVS to Traf2, Traf5, and Traf6 is dependent on virus infection and MAVS polymerization. The TRAF proteins promote ubiquitination that recruits IKBKG binding to the MAVS signalling complex.
Upon viral infection, MAVS recruits MKK7 onto mitochondria, leading to the induction of apoptosis by MAP2K7 activated MAPK9
Macrocyclic NS3-4A resistance-associated amino acid variants (RAVs) with substitutions at residue D168 of the hepatitis C virus protease result in an increased capacity of NS3-4A to cleave MAVS and suppress IFNB1 induction.
RNA cleavage products, catalyzed by RNASEL, bind to DHX33 to facilitate the formation of a complex with MAVS and NLRP3 during viral infection.
HACE1 plays an inhibitory role in virus-induced signalling by disrupting the MAVS-TRAF3 complex.
MARCH5 modulates MAVS-mediated antiviral signalling, preventing excessive immune reactions.
MAVS directly interacts with TRAF6 through its potential TRAF6-binding motif 2.
|InnateDB Annotation from Orthologs
[Mus musculus] The Mavs signalling pathway in non-myeloid cells is crucial for dsRNA-mediated natural killer cell activation.
[Mus musculus] Tyrosine phosphorylation of Mavs at amino acid residue Tyr9 is critical for the induction of Ifnb signalling. (Demonstrated in human)
[Mus musculus] Upon infection with encephalitic Bunyavirus, RIG-I/MAVS signalling activates SARM1 to mediate neuronal cell death.
[Mus musculus] MAVS binds to VDAC1 to trigger viral-induced apoptosis.
[Mus musculus] Plasmodium RNA is a pathogen-associated molecular pattern (PAMP) capable of activating a type I IFN response via the cytosolic pattern recognition receptors Ifih1 and Mavs, as well as via transcription factors Irf3 and Irf7.
[Mus musculus] Antiviral response to rotavirus in infected macrophages is fully Mavs-dependent.
[Mus musculus] Alveolar macrophages detect respiratory syncytial virus (RSV) via the Mavs /Ddx58 pathway and are a major source of type I interferons upon RSV infection.
[Mus musculus] Transgenic picornavirus RNA-dependent RNA polymerase (RdRP) expression in mice produces a quantitatively dramatic, sustained, effective antiviral interferon-stimulated genes (ISG) network, which requires the MDA5-MAVS pathway.
[Mus musculus] March5 modulates Mavs-mediated antiviral signalling, preventing excessive immune reactions.
[Mus musculus] Baiap2l1 recruits Ube2i to sumoylate Pcbp2, which causes its cytoplasmic translocation during viral infection and the sumoylated Pcbp2 associates with Mavs to initiate its degradation, leading to downregulation of antiviral responses.
This gene encodes an intermediary protein necessary in the virus-triggered beta interferon signaling pathways. It is required for activation of transcription factors which regulate expression of beta interferon and contributes to antiviral immunity. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2011]
|Number of Interactions
This gene and/or its encoded proteins are associated with 156 experimentally validated interaction(s) in this database.
They are also associated with 11 interaction(s) predicted by orthology.
Not yet available
TRAF6 mediated IRF7 activation pathway
Negative regulators of RIG-I/MDA5 signaling pathway
TRAF3-dependent IRF activation pathway pathway
TRAF6 mediated NF-kB activation pathway
NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 pathway
RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways pathway
Innate Immune System pathway
Immune System pathway
RIG-I-like receptor signaling pathway pathway
Cytosolic DNA-sensing pathway pathway
Hepatitis C pathway
|UniProt Splice Variant
|AB033097 AB097003 AB232371 AK023799 AK123956 AK130992 AK291785 AK296897 AL109804 AL353194 BC044952 CH471133 DQ167126 DQ174270 DQ181928 EF467323 EF467324
|AAH44952 AAZ80417 ABA19229 ABA54890 ABR24161 ABR24162 BAA86585 BAB14684 BAC77356 BAC85473 BAC85734 BAE79738 BAF84474 BAG59455 CAI11041 CAI18851 EAX10481
|RNA Seq Atlas