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14.3816 -6.5322 c -10.571 2.2124 -2.4899 -6.8115 -5.9681 7.9727 l -29.0256 -4.4044 c -6.096 0.0919 -6.2013 -14.1503 -2.0879 -15.0274 c -1.0542 10.2454 -7.5808 0.1474 6.1282 7.8622 l -13.374 24.8929 c -1.7923 5.5423 -16.0665 1.2366 -15.6721 -2.7553 c 9.9194 4.1194 -2.1948 6.9024 9.7557 -3.1134 l 20.7599 19.7894 c 4.9886 3.3337 -3.7283 14.915 -7.5982 13.3243 c 7.1844 -7.6993 6.2238 4.1184 -0.0987 -9.7867 l 26.2042 -12.6627 c 4.875 -3.4821 13.7627 7.9809 10.9766 10.9902 z" /> </svg> PMID: 16474426, 15208624 retinoic acid inducible gene – I (RIG-I) has been identified as a cytosolic receptor for intracellular dsRNA. indirect PMID: 16474426 In the presence of diverse stimuli, such as IL-1beta, TNF-alpha, and viruses, the IkappaB kinase (IKK) is activated and it then phosphorylates IkappaB. indirect PMID: 16474426 In the presence of diverse stimuli, such as IL-1beta, TNF-alpha, and viruses, the IkappaB kinase (IKK) is activated and it then phosphorylates IkappaB. PMID: 16474426 In the presence of diverse stimuli, such as IL-1beta, TNF-alpha, and viruses, the IkappaB kinase (IKK) is activated and it then phosphorylates IkappaB. PMID: 16474426 Once phosphorylated, IkappaB is ubiquitinated and subsequently degraded by the proteasome. PMID: 16474426 Once phosphorylated, IkappaB is ubiquitinated and subsequently degraded by the proteasome. PMID: 16474426 Free NF-kappaB then translocates into the nucleus and turns on its target genes. PMID: 16474426, 12692549, 12702806 In response to a viral challenge, IRF3 is phosphorylated by the IKK-like kinases TBK-1 and IKKe. PMID: 16474426, 12692549, 12702806 In response to a viral challenge, IRF3 is phosphorylated by the IKK-like kinases TBK-1 and IKKe. PMID: 16474426 Phosphorylation of IRF3 leads to its dimerization and translocation into the nucleus. PMID: 16474426 Phosphorylation of IRF3 leads to its dimerization and translocation into the nucleus. PMID: 16474426 Viral infection also leads to activation of stress kinases such as JNK and p38 kinase, which phosphorylate ATF2/c-Jun in the nucleus. PMID: 16474426 Viral infection also leads to activation of stress kinases such as JNK and p38 kinase, which phosphorylate ATF2/c-Jun in the nucleus. PMID: 16474426 Viral infection also leads to activation of stress kinases such as JNK and p38 kinase, which phosphorylate ATF2/c-Jun in the nucleus. PMID: 16474426 Viral infection also leads to activation of stress kinases such as JNK and p38 kinase, which phosphorylate ATF2/c-Jun in the nucleus. PMID: 16474426 Together with the nuclear architectural protein HMG-I (Y), NF-kappaB, IRF3 and ATF2/c-Jun assemble into a stereospecific enhanceosome complex that remodels the chromatin in the promoter of IFN-beta, resulting in its transcriptional initiation. PMID: 16474426 Together with the nuclear architectural protein HMG-I (Y), NF-kappaB, IRF3 and ATF2/c-Jun assemble into a stereospecific enhanceosome complex that remodels the chromatin in the promoter of IFN-beta, resulting in its transcriptional initiation. PMID: 16474426 Together with the nuclear architectural protein HMG-I (Y), NF-kappaB, IRF3 and ATF2/c-Jun assemble into a stereospecific enhanceosome complex that remodels the chromatin in the promoter of IFN-beta, resulting in its transcriptional initiation. PMID: 16474426, 16214811 IFN-beta binds to the IFNalpha/beta receptor (IFNAR) in autocrine and paracrine manner to initiate a positive feedback loop that results in further production of type I IFNs. indirect PMID: 16474426 IFNARs trigger the activation of the janus kinase (JAK) family members JAK1 and Tyk-2. indirect PMID: 16474426 IFNARs trigger the activation of the janus kinase (JAK) family members JAK1 and Tyk-2. PMID: 16474426 These kinases in turn phosphorylate and activate the signal transducer and activator of transcription 1 (STAT1) and STAT2 proteins. PMID: 16474426 These kinases in turn phosphorylate and activate the signal transducer and activator of transcription 1 (STAT1) and STAT2 proteins. PMID: 16474426 These kinases in turn phosphorylate and activate the signal transducer and activator of transcription 1 (STAT1) and STAT2 proteins. PMID: 16474426 These kinases in turn phosphorylate and activate the signal transducer and activator of transcription 1 (STAT1) and STAT2 proteins. PMID: 16474426 These transcription factors associate with IRF9 to form a heterotrimeric complex, IFN-stimulated gene factor 3 (ISGF3). PMID: 16474426 ISGF3 initiates the transcription of several interferon stimulated genes (ISGs) by binding to the IFN-stimulated response elements (ISRE) in their promoter regions. PMID: 16474426 IFN-beta produced in response to a viral challenge by the IRF3 dependent pathway described above, induces transcription of IRF-7. PMID: 16474426 IFN-beta produced in response to a viral challenge by the IRF3 dependent pathway described above, induces transcription of IRF-7. indirect PMID: 16474426 IFN-beta produced in response to a viral challenge by the IRF3 dependent pathway described above, induces transcription of IRF-7. PMID: 16474426 IRF7 is then activated by phosphorylation at certain key residues by TBK-1/IKKe such that it binds and induces the promoter of IFN-alpha gene. PMID: 16474426 IRF7 is then activated by phosphorylation at certain key residues by TBK-1/IKKe such that it binds and induces the promoter of IFN-alpha gene. PMID: 16474426 IRF7 is then activated by phosphorylation at certain key residues by TBK-1/IKKe such that it binds and induces the promoter of IFN-alpha gene. PMID: 16474426 IRF7 is then activated by phosphorylation at certain key residues by TBK-1/IKKe such that it binds and induces the promoter of IFN-alpha gene. PMID: 16474426 TLR3 recognizes viral double-stranded RNA, TLR4 recognizes bacterial lipopolysaccharides (LPS), whereas TLR5 is a receptor for bacterial flagellin. PMID: 16474426 TLR3 recognizes viral double-stranded RNA, TLR4 recognizes bacterial lipopolysaccharides (LPS), whereas TLR5 is a receptor for bacterial flagellin. PMID: 16474426 Except for TLR3, all TLRs utilize MyD88 as an adaptor protein to recruit downstream signaling molecules including the protein kinases IRAK4 and IRAK1, and the RING domain ubiquitin ligase TRAF6. PMID: 16474426 Except for TLR3, all TLRs utilize MyD88 as an adaptor protein to recruit downstream signaling molecules including the protein kinases IRAK4 and IRAK1, and the RING domain ubiquitin ligase TRAF6. PMID: 16474426, 11057907, 11460167 TRAF6 functions together with a dimeric ubiquitin conjugating enzyme complex Ubc13-Uev1A to catalyze the synthesis of Lys63-linked polyubiquitin chains that lead to the activation of a protein kinase complex consisting of TAK1, TAB1 and TAB2. indirect PMID: 16474426, 11057907, 11460167 TRAF6 functions together with a dimeric ubiquitin conjugating enzyme complex Ubc13-Uev1A to catalyze the synthesis of Lys63-linked polyubiquitin chains that lead to the activation of a protein kinase complex consisting of TAK1, TAB1 and TAB2. PMID: 16474426 The activated TAK1 kinase phosphorylates IKKbeta in the activation loop, resulting in the activation of IKK and subsequent nuclear translocation of NF-kappaB. PMID: 16474426 The TIR domains of TLR3 and TLR4 bind to another adaptor protein TRIF, which binds directly to TRAF6 and RIP1 to activate NF-kappaB. PMID: 16474426 The TIR domains of TLR3 and TLR4 bind to another adaptor protein TRIF, which binds directly to TRAF6 and RIP1 to activate NF-kappaB. PMID: 16474426 The TIR domains of TLR3 and TLR4 bind to another adaptor protein TRIF, which binds directly to TRAF6 and RIP1 to activate NF-kappaB. indirect PMID: 16474426 The TIR domains of TLR3 and TLR4 bind to another adaptor protein TRIF, which binds directly to TRAF6 and RIP1 to activate NF-kappaB. PMID: 16474426 TRIF can also bind to TBK1, which phosphorylates and activates IRF3 and IRF7. PMID: 16474426, 16306937, 16306936 Recent studies have also shown that TRIF and MyD88 can bind to TRAF3. PMID: 16474426, 16306937, 16306936 Recent studies have also shown that TRIF and MyD88 can bind to TRAF3. PMID: 16474426 TLR7 and TLR8 are receptors for G/U-rich ssRNA associated with viruses that enter cells through endocytosis. PMID: 16474426 TLR7 and TLR8 are receptors for G/U-rich ssRNA associated with viruses that enter cells through endocytosis. PMID: 16474426 TLR9 recognizes unmethylated CpG DNA present in DNA viruses such as herpesvirus. PMID: 16474426 It has been shown that MyD88 and TRAF6 can bind to IRF7 directly, and recruit IRAK1 to phosphorylate IRF7, resulting in the nuclear translocation and activation of IRF7. PMID: 16474426 It has been shown that MyD88 and TRAF6 can bind to IRF7 directly, and recruit IRAK1 to phosphorylate IRF7, resulting in the nuclear translocation and activation of IRF7. PMID: 16474426 It has been shown that MyD88 and TRAF6 can bind to IRF7 directly, and recruit IRAK1 to phosphorylate IRF7, resulting in the nuclear translocation and activation of IRF7. PMID: 16474426, 15361868 TRAF6 appears to induce the phosphorylation of IRF7 through a mechanism that involves Ubc13-catalyzed K63 polyubiquitination. PMID: 16474426 It has been shown that MyD88 and TRAF6 can bind to IRF7 directly, and recruit IRAK1 to phosphorylate IRF7, resulting in the nuclear translocation and activation of IRF7. PMID: 16474426 MAVS has been shown to interact with RIG-I in over-expression experiments. PMID: 16474426, 16125763, 16153868 MAVS can interact with TRAF6 and both identified TRAF6 binding sites within MAVS. PMID: 16474426, 16127453 MAVS interacted with RIP-1 and FADD, and proposed that these molecules linked MAVS to IKK activation. indirect PMID: 16474426, 16127453 MAVS interacted with RIP-1 and FADD, and proposed that these molecules linked MAVS to IKK activation. PMID: 16474426 MAVS bound to IKK alpha and IKK-epsilon directly. PMID: 16474426 NS3/4A binds to and co-localizes with MAVS in the mitochondrial membrane, and it can cleave MAVS directly in vitro. PMID: 16474426 MAVS bound to IKK alpha and IKK-epsilon directly. PMID: 16474426 NS3/4A binds to and co-localizes with MAVS in the mitochondrial membrane, and it can cleave MAVS directly in vitro. indirect PMID: 16474426 Over-expression of the N-terminal region of RIG-I comprising the two CARD domains is sufficient to activate NF-kappaB and IRF3 in the absence of a viral challenge, whereas the full-length RIG-I is activated only in the presence of dsRNA. indirect PMID: 16474426 Over-expression of the N-terminal region of RIG-I comprising the two CARD domains is sufficient to activate NF-kappaB and IRF3 in the absence of a viral challenge, whereas the full-length RIG-I is activated only in the presence of dsRNA. PMID: 16474426 TLR3 recognizes viral double-stranded RNA, TLR4 recognizes bacterial lipopolysaccharides (LPS), whereas TLR5 is a receptor for bacterial flagellin.