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style="fill:url(#MO_59ab14);stroke:none;" d="M 60 48.5415 c 0.8103 -7.397 2.3214 -19.8066 -3.5398 -20.1631 c 9.5776 -10.3066 -2.5463 -7.5712 3.5398 -16.9193 c -7.1467 -3.0187 -19.0893 -8.2203 -21.2568 -3.0292 c -7.3468 -11.8479 -8.3579 -0.0366 -15.8253 -8.4299 c -5.2269 5.5315 -14.1193 14.7258 -9.5978 18.2907 c -14.118 2.984 -2.6193 7.5483 -13.3201 11.7096 c 3.9166 6.4373 10.3631 17.3217 15.3246 14.3334 c -1.3787 13.6923 6.7392 4.7019 7.5932 15.6663 c 7.6473 -1.5531 20.5241 -4.0206 19.0691 -9.4324 c 13.2666 5.4782 6.7842 -4.643 18.013 -2.0267 z" /> </svg> PMID: 18549796 The ligands for RIG-I and MDA-5 are viral “nonself” nucleic acids, and like TLR signaling, a classical ligand-receptor-adaptor model of PRR signaling has been proposed for RLH-mediated signaling, culminating in the induction of antiviral type-1 interferon cytokines, such as IFN-β and IFN-α. PMID: 18549796 The ligands for RIG-I and MDA-5 are viral “nonself” nucleic acids, and like TLR signaling, a classical ligand-receptor-adaptor model of PRR signaling has been proposed for RLH-mediated signaling, culminating in the induction of antiviral type-1 interferon cytokines, such as IFN-β and IFN-α. indirect PMID: 18549796 The ligands for RIG-I and MDA-5 are viral “nonself” nucleic acids, and like TLR signaling, a classical ligand-receptor-adaptor model of PRR signaling has been proposed for RLH-mediated signaling, culminating in the induction of antiviral type-1 interferon cytokines, such as IFN-β and IFN-α. indirect PMID: 18549796 The ligands for RIG-I and MDA-5 are viral “nonself” nucleic acids, and like TLR signaling, a classical ligand-receptor-adaptor model of PRR signaling has been proposed for RLH-mediated signaling, culminating in the induction of antiviral type-1 interferon cytokines, such as IFN-β and IFN-α. indirect PMID: 18549796 The ligands for RIG-I and MDA-5 are viral “nonself” nucleic acids, and like TLR signaling, a classical ligand-receptor-adaptor model of PRR signaling has been proposed for RLH-mediated signaling, culminating in the induction of antiviral type-1 interferon cytokines, such as IFN-β and IFN-α. indirect PMID: 18549796 The ligands for RIG-I and MDA-5 are viral “nonself” nucleic acids, and like TLR signaling, a classical ligand-receptor-adaptor model of PRR signaling has been proposed for RLH-mediated signaling, culminating in the induction of antiviral type-1 interferon cytokines, such as IFN-β and IFN-α. PMID: 18549796, 16125763 Upon viral challenge, the MAVS CARD associates with the CARDs of RIG-I or MDA-5. PMID: 18549796, 16125763 Upon viral challenge, the MAVS CARD associates with the CARDs of RIG-I or MDA-5. PMID: 18549796 TRIM25, functions as an E3 ubiquitin ligase of RIG-I. The SPRY domain of TRIM25 delivers a lysine 63-linked ubiquitin moiety to the N-terminal CARDs of RIG-I, which strengthens interactions with MAVS and enhances downstream signaling to IFN-β. PMID: 18549796 NLRX1 was found to interact with MAVS and block RIG-I-MAVS interactions and signaling after Sendai virus infection. PMID: 18549796, 18272355 The MAVS proline-rich domain contains a TRAF3-binding site required for association with TRAF3 and essential for MAVS-mediated activation of type-1 interferon, but not NF-κB. indirect PMID: 18549796, 18272355 The MAVS proline-rich domain contains a TRAF3-binding site required for association with TRAF3 and essential for MAVS-mediated activation of type-1 interferon, but not NF-κB. PMID: 18549796 The deubiquitinizing enzyme A (DUBA) cleaves Lys-63-linked polyubiquitin chains from TRAF3 resulting in the dissociation of TRAF3 from TBK1, and such a dissociation effectively squelches RLH-mediated type-1 interferon production. PMID: 18549796, 16153868 Conversely, mutation of a MAVS TRAF6-binding site showed marked reduction in MAVS-mediated NF-κB activity, suggesting that TRAF6 mediates MAVS activation of NF-κB. indirect PMID: 18549796 MAVS signaling downstream of TRAF6 is thought to involve the activation of the canonical IκB kinase (IKK) complex consisting of IKKγ(NEMO):IKKα:IKKβ, resulting in the phosphorylation of the inhibitor of NF-κB (IκBα) and its subsequent release for translocation into the nucleus. PMID: 18549796 MAVS signaling downstream of TRAF6 is thought to involve the activation of the canonical IκB kinase (IKK) complex consisting of IKKγ(NEMO):IKKα:IKKβ, resulting in the phosphorylation of the inhibitor of NF-κB (IκBα) and its subsequent release for translocation into the nucleus. PMID: 18549796 MAVS signaling downstream of TRAF6 is thought to involve the activation of the canonical IκB kinase (IKK) complex consisting of IKKγ(NEMO):IKKα:IKKβ, resulting in the phosphorylation of the inhibitor of NF-κB (IκBα) and its subsequent release for translocation into the nucleus. PMID: 18549796 MAVS signaling downstream of TRAF6 is thought to involve the activation of the canonical IκB kinase (IKK) complex consisting of IKKγ(NEMO):IKKα:IKKβ, resulting in the phosphorylation of the inhibitor of NF-κB (IκBα) and its subsequent release for translocation into the nucleus. PMID: 18549796 In contrast, MAVS signaling downstream of TRAF3 involves the formation and activation of a different signaling complex consisting of MAVS, the TRAF-family-member-associated NF-κB activator (TANK), and a noncanonical class of IKKs including (TANK)-binding kinase 1 (TBK1) and inducible IκB kinase (IKK-í or IKK-var epsilon). PMID: 18549796 The deubiquitinizing enzyme A (DUBA) cleaves Lys-63-linked polyubiquitin chains from TRAF3 resulting in the dissociation of TRAF3 from TBK1, and such a dissociation effectively squelches RLH-mediated type-1 interferon production. PMID: 18549796 In contrast, MAVS signaling downstream of TRAF3 involves the formation and activation of a different signaling complex consisting of MAVS, the TRAF-family-member-associated NF-κB activator (TANK), and a noncanonical class of IKKs including (TANK)-binding kinase 1 (TBK1) and inducible IκB kinase (IKK-í or IKK-var epsilon). PMID: 18549796 The activation of TBK1 and IKK-í results in the phosphorylation and subsequent dimerization and nuclear translocation of the transcription factors IRF3 and IRF7. PMID: 18549796, 17079289 NS1 was found to complex with RIG-I and associate with MAVS at the mitochondria, thereby disrupting downstream activation of IRF-3. PMID: 18549796 The activation of TBK1 and IKK-í results in the phosphorylation and subsequent dimerization and nuclear translocation of the transcription factors IRF3 and IRF7. PMID: 18549796 The activation of TBK1 and IKK-í results in the phosphorylation and subsequent dimerization and nuclear translocation of the transcription factors IRF3 and IRF7. PMID: 18549796 The activation of TBK1 and IKK-í results in the phosphorylation and subsequent dimerization and nuclear translocation of the transcription factors IRF3 and IRF7. PMID: 18549796 The activation of TBK1 and IKK-í results in the phosphorylation and subsequent dimerization and nuclear translocation of the transcription factors IRF3 and IRF7. PMID: 18549796 The activation of TBK1 and IKK-í results in the phosphorylation and subsequent dimerization and nuclear translocation of the transcription factors IRF3 and IRF7. PMID: 18549796 Because it is known that both NF-κB and IRF3 and IRF7 are required for the assembly of an enhancesome complex required for the induction of IFN-β and IFN-α promoters, the essential role of MAVS in the activation of both of these transcription factors further emphasizes the importance of this mitochondrial adaptor protein in type-1 interferon signaling. PMID: 18549796 Because it is known that both NF-κB and IRF3 and IRF7 are required for the assembly of an enhancesome complex required for the induction of IFN-β and IFN-α promoters, the essential role of MAVS in the activation of both of these transcription factors further emphasizes the importance of this mitochondrial adaptor protein in type-1 interferon signaling. indirect PMID: 18549796, 18272355 The MAVS proline-rich domain contains a TRAF3-binding site required for association with TRAF3 and essential for MAVS-mediated activation of type-1 interferon, but not NF-κB. indirect PMID: 18549796 In fact, RIG-I-mediated production of IFN can, in turn, increase the transcription of RIG-I itself, thus setting into motion an IFN amplification loop, which if left unchecked, could become deleterious to the host. indirect PMID: 18549796, 18262678 similar to RIG-I, LGP2 is inducible by IFN-β, virus, or dsRNA and can bind viral RNA through a RIG-I-like C-terminal domain. indirect PMID: 18549796, 18262678 similar to RIG-I, LGP2 is inducible by IFN-β, virus, or dsRNA and can bind viral RNA through a RIG-I-like C-terminal domain. PMID: 18549796, 18262678 similar to RIG-I, LGP2 is inducible by IFN-β, virus, or dsRNA and can bind viral RNA through a RIG-I-like C-terminal domain. PMID: 18549796 Another intriguing property of LGP2 is its ability to associate with MAVS despite the loss of CARDs. PMID: 18549796 LGP2 contains a RIG-I-like repression domain (RD) capable of inhibiting RIG-I multimerization and signaling. PMID: 18549796, 17460044 The IFN-inducible ubiquitin ligase RNF125 was found to conjugate lysine 48-linked polyubiquitin chains to RIG-I or MDA-5 and cause the proteosomal degradation of either protein. PMID: 18549796, 17460044 The IFN-inducible ubiquitin ligase RNF125 was found to conjugate lysine 48-linked polyubiquitin chains to RIG-I or MDA-5 and cause the proteosomal degradation of either protein. PMID: 18549796, 17460044 The IFN-inducible ubiquitin ligase RNF125 was found to conjugate lysine 48-linked polyubiquitin chains to RIG-I or MDA-5 and cause the proteosomal degradation of either protein. PMID: 18549796, 16699525 Upon transfection with dsRNA, the peptidyl-prolyl isomerase (Pin1) interacts with phosphorylated IRF3, resulting in the proteasomal degradation of IRF3. PMID: 18549796, 16699525 Upon transfection with dsRNA, the peptidyl-prolyl isomerase (Pin1) interacts with phosphorylated IRF3, resulting in the proteasomal degradation of IRF3. PMID: 18549796 TRIM25, functions as an E3 ubiquitin ligase of RIG-I. The SPRY domain of TRIM25 delivers a lysine 63-linked ubiquitin moiety to the N-terminal CARDs of RIG-I, which strengthens interactions with MAVS and enhances downstream signaling to IFN-β. PMID: 18549796 The deubiquitinizing enzyme A (DUBA) cleaves Lys-63-linked polyubiquitin chains from TRAF3 resulting in the dissociation of TRAF3 from TBK1, and such a dissociation effectively squelches RLH-mediated type-1 interferon production. PMID: 18549796 The deubiquitinizing enzyme A (DUBA) cleaves Lys-63-linked polyubiquitin chains from TRAF3 resulting in the dissociation of TRAF3 from TBK1, and such a dissociation effectively squelches RLH-mediated type-1 interferon production. PMID: 18549796 The deubiquitinizing enzyme A (DUBA) cleaves Lys-63-linked polyubiquitin chains from TRAF3 resulting in the dissociation of TRAF3 from TBK1, and such a dissociation effectively squelches RLH-mediated type-1 interferon production. PMID: 18549796 In the absence of viral infection, the Atg5-Atg12 conjugate interacts directly with the MAVS CARD and weakly associated with RIG-I and MDA-5 CARDs. PMID: 18549796 In the absence of viral infection, the Atg5-Atg12 conjugate interacts directly with the MAVS CARD and weakly associated with RIG-I and MDA-5 CARDs. PMID: 18549796 In the absence of viral infection, the Atg5-Atg12 conjugate interacts directly with the MAVS CARD and weakly associated with RIG-I and MDA-5 CARDs. PMID: 18549796 NLRX1 was found to interact with MAVS and block RIG-I-MAVS interactions and signaling after Sendai virus infection. indirect PMID: 18549796, 18219313 Reactive oxygen species (ROS) production is increased with NLRX1 overexpression. PMID: 18549796, 18272355 Each of these RNA viruses encode for a V protein that binds to MDA-5 and inhibits dsRNA or MDA-5 induction of IFN-β promoter activity. PMID: 18549796, 17438296 This virus targets the RIG-I pathway downstream of RIG-I and upstream of the TBK1-IKK-var epsilon complex by cleaving MAVS utilizing a virally encoded protease, 3ABC. PMID: 18549796 NS3/4A, colocalizes with MAVS at the mitochondria and specifically targets MAVS as a means to inhibit IFN production. PMID: 18549796, 18272355 NS3/4A contains serine-protease activity that proteolytically cleaves MAVS at the cysteine-508 resulting in the loss of MAVS mitochondrial localization. PMID: 18549796 Interestingly, NS3/4A also cleaves TRIF, the essential adaptor of TLR3-signaling, thereby extending the IFN inhibitory properties of HCV to TLR-mediated responses. PMID: 18549796, 17079289 NS1 was found to complex with RIG-I and associate with MAVS at the mitochondria, thereby disrupting downstream activation of IRF-3. PMID: 18549796, 17079289 NS1 was found to complex with RIG-I and associate with MAVS at the mitochondria, thereby disrupting downstream activation of IRF-3. PMID: 18549796, 16125763 Upon viral challenge, the MAVS CARD associates with the CARDs of RIG-I or MDA-5. PMID: 18549796 TRIM25, functions as an E3 ubiquitin ligase of RIG-I. The SPRY domain of TRIM25 delivers a lysine 63-linked ubiquitin moiety to the N-terminal CARDs of RIG-I, which strengthens interactions with MAVS and enhances downstream signaling to IFN-β. PMID: 18549796 NLRX1 was found to interact with MAVS and block RIG-I-MAVS interactions and signaling after Sendai virus infection. PMID: 18549796 Because it is known that both NF-κB and IRF3 and IRF7 are required for the assembly of an enhancesome complex required for the induction of IFN-β and IFN-α promoters, the essential role of MAVS in the activation of both of these transcription factors further emphasizes the importance of this mitochondrial adaptor protein in type-1 interferon signaling. PMID: 18549796 Because it is known that both NF-κB and IRF3 and IRF7 are required for the assembly of an enhancesome complex required for the induction of IFN-β and IFN-α promoters, the essential role of MAVS in the activation of both of these transcription factors further emphasizes the importance of this mitochondrial adaptor protein in type-1 interferon signaling.