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-2.9523 c 2.743 7.2454 4.1958 10.1682 5.3676 -8.7112 z" /> </svg> <svg contentScriptType="text/ecmascript" width="60.0" xmlns:xlink="http://www.w3.org/1999/xlink" zoomAndPan="magnify" style="overflow:visible;enable-background:new 0 0 60.0 60.0" contentStyleType="text/css" height="60.0" viewBox="0 0 60.0 60.0" preserveAspectRatio="xMidYMid meet" xmlns="http://www.w3.org/2000/svg" version="1.0"> <defs> <radialGradient id="MO_ab834f" gradientUnits="objectBoundingBox" spreadMethod="pad" xlink:show="other" xlink:type="simple" r="50%" cx="50%" fx="50%" fy="50%" cy="50%" xlink:actuate="onLoad"> <stop offset="0%" style="stop-color:white;stop-opacity:1;"/> <stop offset="100%" style="stop-color:#ab834f;stop-opacity:1;"/> </radialGradient> </defs> <path style="fill:url(#MO_ab834f);stroke:none;" d="M 60 30 l -34.9569 -27.9966 l -17.8713 -2.0034 l -7.1718 43.775 l 7.1718 16.225 l 42.128 -15.7784 l 10.7001 -14.2216 z" /> </svg> PMID: 18353649,16822173 These include lipopolysaccharide (LPS), a component of the outer membrane of Gram-negative bacteria, and double-stranded (ds) RNA, a product of many replicating viruses, which trigger the TLR4- or the TLR3-dependent signaling cascade, respectively PMID: 18353649,16822173 These include lipopolysaccharide (LPS), a component of the outer membrane of Gram-negative bacteria, and double-stranded (ds) RNA, a product of many replicating viruses, which trigger the TLR4- or the TLR3-dependent signaling cascade, respectively PMID: 18353649,12471095,12539043 Both pathways requires Toll–IL-1 receptor (TIR) domain-containing adaptor inducing IFN-β (TRIF) [also called TIR-containing adapter molecule-1 (TICAM-1)] and one of the five TIR-domain-containing adaptors identified so far PMID: 18353649,12471095,12539043 Both pathways requires Toll–IL-1 receptor (TIR) domain-containing adaptor inducing IFN-β (TRIF) [also called TIR-containing adapter molecule-1 (TICAM-1)] and one of the five TIR-domain-containing adaptors identified so far PMID: 18353649,16621716,16582590,16306937,16306936 TRAF3, which connects TRIF to the TBK1 and IKK-var epsilon kinase complexes for subsequent IRF3 phosphorylation, lies downstream of TRIF PMID: 18353649, 16424890 The TLR7, TLR8 and TLR9 receptors, which, in contrast to TLR4, are not localized on the cell surface but rather in endosomal compartments, sense viral nucleic acids in plasmacytoid dendritic cells and also elicit IFN gene induction through IRF7 phosphorylation PMID: 18353649, 16424890 The TLR7, TLR8 and TLR9 receptors, which, in contrast to TLR4, are not localized on the cell surface but rather in endosomal compartments, sense viral nucleic acids in plasmacytoid dendritic cells and also elicit IFN gene induction through IRF7 phosphorylation PMID: 18353649, 16424890 The TLR7, TLR8 and TLR9 receptors, which, in contrast to TLR4, are not localized on the cell surface but rather in endosomal compartments, sense viral nucleic acids in plasmacytoid dendritic cells and also elicit IFN gene induction through IRF7 phosphorylation PMID: 18353649,10759890 TANK constitutively binds to IKK-epsilon and TBK1 through its N-terminal domain PMID: 18353649,14560022 NAP1, a candidate scaffold protein that was initially identified as a TBK1-interacting protein, shares several structural features with TANK PMID: 18353649,15611223,17142768 Similarly to TANK, NAP1 constitutively binds to TBK1 and is also required for IRF3 phosphorylation through both the TLR3- and the RIG-I-dependent pathways PMID: 18353649,17568778 SINTBAD is the most recently identified scaffold protein that constitutively binds to TBK1 and IKK-epsilon PMID: 18353649 The IRF3-activating pathway also involves TRAF3; this connects TRIF to the TBK1–IKK-epsilon heterodimer kinase complex, which is assembled by the scaffold protein NAP1 PMID: 18353649 Of note, however, IRF7 was also identified as a TANK-interacting protein through yeast two-hybrid analyses, and IRF7 can be phosphorylated by TANK-containing immune complexes in macrophages treated with unmethylated CpG DNA motifs, which are TLR9 ligands PMID: 18353649,17468758 This hypothesis is supported by the physical association between TANK and NEMO PMID: 18353649,16621716,16582590,16306937,16306936 TRAF3, which connects TRIF to the TBK1 and IKK-var epsilon kinase complexes for subsequent IRF3 phosphorylation, lies downstream of TRIF PMID: 18353649 The IRF3-activating pathway also involves TRAF3; this connects TRIF to the TBK1–IKK-epsilon heterodimer kinase complex, which is assembled by the scaffold protein NAP1 indirect PMID: 18353649 IRF3 is phosphorylated (P) within its C-terminal domain by TBK1–IKK-epsilon and forms a homodimer which translocates to the nucleus, binds to ISREs and induces the expression of IFN-dependent genes. PMID: 18353649 IRF3 is phosphorylated (P) within its C-terminal domain by TBK1–IKK-epsilon and forms a homodimer which translocates to the nucleus, binds to ISREs and induces the expression of IFN-dependent genes. PMID: 18353649 IRF3 is phosphorylated (P) within its C-terminal domain by TBK1–IKK-epsilon and forms a homodimer which translocates to the nucleus, binds to ISREs and induces the expression of IFN-dependent genes. PMID: 18353649,15258597,15661910 For example, the TNF-alpha-inducible A20 protein negatively regulates both NF-κB and IRF3-activating pathways by promoting the K48-linked, degradative polyubiquitylation of the receptor-interacting protein (RIP1) in TNF-alpha-stimulated cells or by preventing IRF3 dimerization through direct binding to TBK1 and IKK-var epsilon in dsRNA-stimulated or Newcastle virus-infected cells, respectively PMID: 18353649 IRF3 is phosphorylated (P) within its C-terminal domain by TBK1–IKK-epsilon and forms a homodimer which translocates to the nucleus, binds to ISREs and induces the expression of IFN-dependent genes. indirect PMID: 18353649 IRF3 is phosphorylated (P) within its C-terminal domain by TBK1–IKK-epsilon and forms a homodimer which translocates to the nucleus, binds to ISREs and induces the expression of IFN-dependent genes. PMID: 18353649 RIP1 and TRAF6 are recruited to TRIF, and the signal-induced polyubiquitylated RIP1 is subsequently recruited to the TAB2–TAK1 signaling complex, a crucial step for IKK activation PMID: 18353649 RIP1 and TRAF6 are recruited to TRIF, and the signal-induced polyubiquitylated RIP1 is subsequently recruited to the TAB2–TAK1 signaling complex, a crucial step for IKK activation PMID: 18353649 RIP1 and TRAF6 are recruited to TRIF, and the signal-induced polyubiquitylated RIP1 is subsequently recruited to the TAB2–TAK1 signaling complex, a crucial step for IKK activation PMID: 18353649 RIP1 and TRAF6 are recruited to TRIF, and the signal-induced polyubiquitylated RIP1 is subsequently recruited to the TAB2–TAK1 signaling complex, a crucial step for IKK activation PMID: 18353649 RIP1 and TRAF6 are recruited to TRIF, and the signal-induced polyubiquitylated RIP1 is subsequently recruited to the TAB2–TAK1 signaling complex, a crucial step for IKK activation PMID: 18353649 The IKK complex is assembled by NEMO and targets IκB alpha for phosphorylation and subsequent degradative polyubiquitylation. indirect PMID: 18353649 RIP1 and TRAF6 are recruited to TRIF, and the signal-induced polyubiquitylated RIP1 is subsequently recruited to the TAB2–TAK1 signaling complex, a crucial step for IKK activation PMID: 18353649 The IKK complex is assembled by NEMO and targets IκB alpha for phosphorylation and subsequent degradative polyubiquitylation. PMID: 18353649 The p50–p65 heterodimer is then released from IκB alpha, moves into the nucleus and induces the expression of various proinflammatory genes through binding to κB sites PMID: 18353649 The p50–p65 heterodimer is then released from IκB alpha, moves into the nucleus and induces the expression of various proinflammatory genes through binding to κB sites PMID: 18353649 The IKK complex is assembled by NEMO and targets IκB alpha for phosphorylation and subsequent degradative polyubiquitylation. PMID: 18353649 TNF-alpha triggers NF-κB activation through TRADD and the classical, NEMO-dependent pathway, which involves IKK-β-mediated IκBgreek small letter alpha phosphorylation and subsequent degradation. PMID: 18353649 The IKK complex is assembled by NEMO and targets IκB alpha for phosphorylation and subsequent degradative polyubiquitylation. PMID: 18353649 TNF-alpha triggers NF-κB activation through TRADD and the classical, NEMO-dependent pathway, which involves IKK-β-mediated IκBgreek small letter alpha phosphorylation and subsequent degradation. PMID: 18353649 The IKK complex is assembled by NEMO and targets IκB alpha for phosphorylation and subsequent degradative polyubiquitylation. PMID: 18353649 TNF-alpha triggers NF-κB activation through TRADD and the classical, NEMO-dependent pathway, which involves IKK-β-mediated IκBgreek small letter alpha phosphorylation and subsequent degradation. PMID: 18353649 The p50–p65 heterodimer is then released from IκB alpha, moves into the nucleus and induces the expression of various proinflammatory genes through binding to κB sites PMID: 18353649 The p50–p65 heterodimer translocates into the nucleus to drive the expression of multiple genes, including TANK, IKK-epsilon and A20. PMID: 18353649 The p50–p65 heterodimer is then released from IκB alpha, moves into the nucleus and induces the expression of various proinflammatory genes through binding to κB sites PMID: 18353649,16621716,16582590,16306937,16306936 TRAF3, which connects TRIF to the TBK1 and IKK-var epsilon kinase complexes for subsequent IRF3 phosphorylation, lies downstream of TRIF PMID: 18353649 IRF3 activation also requires TRAF3, which binds to TANK, the scaffold protein that assembles the TBK1–IKK-epsilon heterodimer indirect PMID: 18353649 IRF3 is phosphorylated (P) within its C-terminal domain by TBK1–IKK-epsilon and forms a homodimer which translocates to the nucleus, binds to ISREs and induces the expression of IFN-dependent genes. PMID: 18353649 LPS and IKK-mediated NF-κB activation occurs through the recruitment of Tollip, Mal and Myd88 followed by the binding of the kinase IRAK1 to TLR4 PMID: 18353649 LPS and IKK-mediated NF-κB activation occurs through the recruitment of Tollip, Mal and Myd88 followed by the binding of the kinase IRAK1 to TLR4 PMID: 18353649 LPS and IKK-mediated NF-κB activation occurs through the recruitment of Tollip, Mal and Myd88 followed by the binding of the kinase IRAK1 to TLR4 PMID: 18353649 LPS and IKK-mediated NF-κB activation occurs through the recruitment of Tollip, Mal and Myd88 followed by the binding of the kinase IRAK1 to TLR4 indirect PMID: 18353649 IRAK1 is subsequently phosphorylated by IRAK4 PMID: 18353649 This event triggers the recruitment of TRAF6 to the receptor complex and subsequent signal-induced association of these proteins with the TAB2–TAB3–TAK1 complex, a step required for IKK activation PMID: 18353649 This event triggers the recruitment of TRAF6 to the receptor complex and subsequent signal-induced association of these proteins with the TAB2–TAB3–TAK1 complex, a step required for IKK activation PMID: 18353649 This event triggers the recruitment of TRAF6 to the receptor complex and subsequent signal-induced association of these proteins with the TAB2–TAB3–TAK1 complex, a step required for IKK activation indirect PMID: 18353649 This event triggers the recruitment of TRAF6 to the receptor complex and subsequent signal-induced association of these proteins with the TAB2–TAB3–TAK1 complex, a step required for IKK activation PMID: 18353649,16039576 Both proteins harbor a DEx(D/H) box RNA helicase domain that is required to sense dsRNA synthesized from replicating virus entering the cytoplasm (e.g. the Sendai virus, the Newcastle disease virus or the vesicular stomatitis virus PMID: 18353649 RNA from viruses triggers the activation of the cytosolic receptors RIG-I and MDA-5 through binding to their DExD/H box RNA helicase PMID: 18353649,16039576 Both proteins harbor a DEx(D/H) box RNA helicase domain that is required to sense dsRNA synthesized from replicating virus entering the cytoplasm (e.g. the Sendai virus, the Newcastle disease virus or the vesicular stomatitis virus PMID: 18353649 RNA from viruses triggers the activation of the cytosolic receptors RIG-I and MDA-5 through binding to their DExD/H box RNA helicase indirect PMID: 18353649 The CARD domains of these receptors subsequently undergo K63-linked polyubiquitylation by the E3 ubiquitin ligase TRIM25, which might facilitate the interaction of RIG-I with the mitochondrial adaptor MAVS. indirect PMID: 18353649 The CARD domains of these receptors subsequently undergo K63-linked polyubiquitylation by the E3 ubiquitin ligase TRIM25, which might facilitate the interaction of RIG-I with the mitochondrial adaptor MAVS. PMID: 18353649 The CARD domains of these receptors subsequently undergo K63-linked polyubiquitylation by the E3 ubiquitin ligase TRIM25, which might facilitate the interaction of RIG-I with the mitochondrial adaptor MAVS. PMID: 18353649,16125763 Because they also harbor two caspase-recruitment domain (CARD)-like domains, they can transmit the signal through direct binding to mitochondrial antiviral signaling (MAVS) PMID: 18353649 The CARD domains of these receptors subsequently undergo K63-linked polyubiquitylation by the E3 ubiquitin ligase TRIM25, which might facilitate the interaction of RIG-I with the mitochondrial adaptor MAVS. PMID: 18353649,16125763 Because they also harbor two caspase-recruitment domain (CARD)-like domains, they can transmit the signal through direct binding to mitochondrial antiviral signaling (MAVS) PMID: 18353649 Indeed, the intracellular DNA sensor is DNA-dependent activator of IFN-regulatory factors (DAI), which binds to, and is activated by, DNA from various sources indirect PMID: 18353649 MAVS signals to TRAF3, which triggers IRF3 phosphorylation through TBK1 and IKK-epsilon-mediated activations. indirect PMID: 18353649 MAVS signals to TRAF3, which triggers IRF3 phosphorylation through TBK1 and IKK-epsilon-mediated activations. PMID: 18353649 MAVS signals to TRAF3, which triggers IRF3 phosphorylation through TBK1 and IKK-epsilon-mediated activations. indirect PMID: 18353649 MAVS signals to TRAF3, which triggers IRF3 phosphorylation through TBK1 and IKK-epsilon-mediated activations. PMID: 18353649 MAVS signals to TRAF3, which triggers IRF3 phosphorylation through TBK1 and IKK-epsilon-mediated activations. PMID: 18353649 MAVS signals to TRAF3, which triggers IRF3 phosphorylation through TBK1 and IKK-epsilon-mediated activations. indirect PMID: 18353649 MAVS signals to TRAF3, which triggers IRF3 phosphorylation through TBK1 and IKK-epsilon-mediated activations. indirect PMID: 18353649 MAVS signals to TRAF3, which triggers IRF3 phosphorylation through TBK1 and IKK-epsilon-mediated activations. indirect PMID: 18353649,16153868,16125763 This protein subsequently triggers NF-κB activation through TRAF6 and the IKK-alpha–beta complex or IRF3 and IRF7 activation through TRAF3 and the TBK1 and IKK-epsilon kinase complexes indirect PMID: 18353649,16153868,16125763 This protein subsequently triggers NF-κB activation through TRAF6 and the IKK-alpha–beta complex or IRF3 and IRF7 activation through TRAF3 and the TBK1 and IKK-epsilon kinase complexes indirect PMID: 18353649,16153868,16125763 This protein subsequently triggers NF-κB activation through TRAF6 and the IKK-alpha–beta complex or IRF3 and IRF7 activation through TRAF3 and the TBK1 and IKK-epsilon kinase complexes indirect PMID: 18353649 Of note, MAVS can also signal to TRAF6 for the IKK-alpha–IKK-beta-complex-mediated NF-κB activation PMID: 18353649,16153868,16125763 This protein subsequently triggers NF-κB activation through TRAF6 and the IKK-alpha–beta complex or IRF3 and IRF7 activation through TRAF3 and the TBK1 and IKK-epsilon kinase complexes PMID: 18353649 Of note, MAVS can also signal to TRAF6 for the IKK-alpha–IKK-beta-complex-mediated NF-κB activation PMID: 18353649,16153868,16125763 This protein subsequently triggers NF-κB activation through TRAF6 and the IKK-alpha–beta complex or IRF3 and IRF7 activation through TRAF3 and the TBK1 and IKK-epsilon kinase complexes indirect PMID: 18353649 Of note, MAVS can also signal to TRAF6 for the IKK-alpha–IKK-beta-complex-mediated NF-κB activation PMID: 18353649,16153868,16125763 This protein subsequently triggers NF-κB activation through TRAF6 and the IKK-alpha–beta complex or IRF3 and IRF7 activation through TRAF3 and the TBK1 and IKK-epsilon kinase complexes indirect PMID: 18353649 Of note, MAVS can also signal to TRAF6 for the IKK-alpha–IKK-beta-complex-mediated NF-κB activation PMID: 18353649,16153868,16125763 This protein subsequently triggers NF-κB activation through TRAF6 and the IKK-alpha–beta complex or IRF3 and IRF7 activation through TRAF3 and the TBK1 and IKK-epsilon kinase complexes PMID: 18353649,17618271 DAI subsequently recruits TBK1, which triggers IRF3 phosphorylation and type I IFN gene expression indirect PMID: 18353649,17618271 DAI subsequently recruits TBK1, which triggers IRF3 phosphorylation and type I IFN gene expression indirect PMID: 18353649,17618271 DAI subsequently recruits TBK1, which triggers IRF3 phosphorylation and type I IFN gene expression PMID: 18353649,17003035 Additional evidence for crosstalk between the two signaling pathways is provided by IKK-var epsilon-mediated phosphorylation of p65 in TNF-alpha-stimulated cells PMID: 18353649,17003035 Additional evidence for crosstalk between the two signaling pathways is provided by IKK-var epsilon-mediated phosphorylation of p65 in TNF-alpha-stimulated cells indirect PMID: 18353649 TNF-alpha triggers NF-κB activation through TRADD and the classical, NEMO-dependent pathway, which involves IKK-β-mediated IκBgreek small letter alpha phosphorylation and subsequent degradation. PMID: 18353649 For example, the TNF-alpha-inducible A20 protein negatively regulates both NF-κB and IRF3-activating pathways by promoting the K48-linked, degradative polyubiquitylation of the receptor-interacting protein (RIP1) in TNF-alpha-stimulated cells indirect PMID: 18353649 The p50–p65 heterodimer translocates into the nucleus to drive the expression of multiple genes, including TANK, IKK-epsilon and A20. indirect PMID: 18353649 The p50–p65 heterodimer translocates into the nucleus to drive the expression of multiple genes, including TANK, IKK-epsilon and A20. indirect PMID: 18353649 The p50–p65 heterodimer translocates into the nucleus to drive the expression of multiple genes, including TANK, IKK-epsilon and A20. indirect PMID: 18353649 The p50–p65 heterodimer translocates into the nucleus to drive the expression of multiple genes, including TANK, IKK-epsilon and A20. indirect PMID: 18353649 For example, the TNF-alpha-inducible A20 protein negatively regulates both NF-κB and IRF3-activating pathways by promoting the K48-linked, degradative polyubiquitylation of the receptor-interacting protein (RIP1) in TNF-alpha-stimulated cells PMID: 18353649 For example, the TNF-alpha-inducible A20 protein negatively regulates both NF-κB and IRF3-activating pathways by promoting the K48-linked, degradative polyubiquitylation of the receptor-interacting protein (RIP1) in TNF-alpha-stimulated cells PMID: 18353649,15258597,15661910 For example, the TNF-alpha-inducible A20 protein negatively regulates both NF-κB and IRF3-activating pathways by promoting the K48-linked, degradative polyubiquitylation of the receptor-interacting protein (RIP1) in TNF-alpha-stimulated cells or by preventing IRF3 dimerization through direct binding to TBK1 and IKK-var epsilon in dsRNA-stimulated or Newcastle virus-infected cells, respectively PMID: 18353649 A second crosstalk is established between IKK-epsilon and p100, an inhibitory molecule whose processing into p52 is triggered following stimulation with lymphotoxin-β PMID: 18353649 p100 is subsequently processed into p52 and moves into the nucleus as a heterodimer with the NF-κB protein RelB PMID: 18353649 A second crosstalk is established between IKK-epsilon and p100, an inhibitory molecule whose processing into p52 is triggered following stimulation with lymphotoxin-β PMID: 18353649 IKK-epsilon expression is also induced in TNF-alpha-stimulated cells, and this kinase associates with p100 and p52 to enhance the transactivation potential of specific p52–p65 heterodimers indirect indirect PMID: 18353649 This pathway, which requires TRAF2 and TRAF5 and is negatively regulated by TRAF3, triggers NIK activation and IKK-alpha-mediated p100 phosphorylation indirect indirect indirect PMID: 18353649 This pathway, which requires TRAF2 and TRAF5 and is negatively regulated by TRAF3, triggers NIK activation and IKK-alpha-mediated p100 phosphorylation. PMID: 18353649 p100 is subsequently processed into p52 and moves into the nucleus as a heterodimer with the NF-κB protein RelB PMID: 18353649 p100 is subsequently processed into p52 and moves into the nucleus as a heterodimer with the NF-κB protein RelB PMID: 18353649 TANK also connects IKK-var epsilon and TBK1 to the IKK complex through binding to NEMO for subsequent p65 phosphorylation indirect indirect PMID: 18353649 TBK1 and IKK-var epsilon phosphorylate TANK in macrophages and also are required for LPS-mediated TANK polyubiquitylation, independently of their kinase activity. indirect indirect PMID: 18353649 TBK1 and IKK-var epsilon phosphorylate TANK in macrophages and also are required for LPS-mediated TANK polyubiquitylation, independently of their kinase activity. PMID: 18353649 TBK1 and IKK-var epsilon phosphorylate TANK in macrophages and also are required for LPS-mediated TANK polyubiquitylation, independently of their kinase activity.