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PMID: 16979567,15208624,16116171 Recently, RIG-I and MDA5 have been identified as essential cytosolic receptors for intracellular viral RNAs and synthetic dsRNAs, mediating the TLR-independent induction of type I IFN genes

PMID: 16979567,15208624,16116171 Recently, RIG-I and MDA5 have been identified as essential cytosolic receptors for intracellular viral RNAs and synthetic dsRNAs, mediating the TLR-independent induction of type I IFN genes

PMID: 16979567 This CARD mediates CARD-CARD interactions with RIG-I and MDA5 and transmits downstream signaling

PMID: 16979567 This CARD mediates CARD-CARD interactions with RIG-I and MDA5 and transmits downstream signaling

PMID: 16979567,16127453,16153868 IPS-1 has been shown to interact with several signaling proteins, such as tumor necrosis factor receptor-associated factor 2 (TRAF2), TRAF6, Fas-associated protein with the death domain (FADD), and receptor interacting protein-1 (RIP1)

PMID: 16979567,16127453,16153868 IPS-1 has been shown to interact with several signaling proteins, such as tumor necrosis factor receptor-associated factor 2 (TRAF2), TRAF6, Fas-associated protein with the death domain (FADD), and receptor interacting protein-1 (RIP1)

indirect

PMID: 16979567 The conformational change promotes the interaction between the RIG-I and MDA5 CARDs and the CARD-containing adaptor protein IPS-1, which is located on the mitochondrial membrane, resulting in the activation of TBK1 via TRAF3 as well as IKK complex via FADD, RIP1 (not depicted), and TRAF6.T

indirect

PMID: 16979567 The conformational change promotes the interaction between the RIG-I and MDA5 CARDs and the CARD-containing adaptor protein IPS-1, which is located on the mitochondrial membrane, resulting in the activation of TBK1 via TRAF3 as well as IKK complex via FADD, RIP1 (not depicted), and TRAF6.T

PMID: 16979567,16858409 Considering the fact that TRAF3 interacts with IPS-1 , TRAF3 probably provides a link between IPS-1 and TBK1 (Figure 2). PMID: 16979567 The conformational change promotes the interaction between the RIG-I and MDA5 CARDs and the CARD-containing adaptor protein IPS-1, which is located on the mitochondrial membrane, resulting in the activation of TBK1 via TRAF3 as well as IKK complex via FADD, RIP1 (not depicted), and TRAF6.

PMID: 16979567,16858409 Considering the fact that TRAF3 interacts with IPS-1 , TRAF3 probably provides a link between IPS-1 and TBK1 (Figure 2). PMID: 16979567 The conformational change promotes the interaction between the RIG-I and MDA5 CARDs and the CARD-containing adaptor protein IPS-1, which is located on the mitochondrial membrane, resulting in the activation of TBK1 via TRAF3 as well as IKK complex via FADD, RIP1 (not depicted), and TRAF6.

indirect

PMID: 16979567 The conformational change promotes the interaction between the RIG-I and MDA5 CARDs and the CARD-containing adaptor protein IPS-1, which is located on the mitochondrial membrane, resulting in the activation of TBK1 via TRAF3 as well as IKK complex via FADD, RIP1 (not depicted), and TRAF6.

indirect

PMID: 16979567 The conformational change promotes the interaction between the RIG-I and MDA5 CARDs and the CARD-containing adaptor protein IPS-1, which is located on the mitochondrial membrane, resulting in the activation of TBK1 via TRAF3 as well as IKK complex via FADD, RIP1 (not depicted), and TRAF6.

indirect

PMID: 16979567, 15210742 Inducible IκB kinase (IKKi; also known as IKKε), which is structurally related to TBK1, was also shown to phosphorylate IRF3 and IRF7 in vitro; however, gene-targeting studies revealed that the contribution of IKKi to the cytosolic pathway is minor

indirect

PMID: 16979567 Activated TBK1 induces the phosphorylation (P−) of IRF3 and IRF7, resulting in their homo- or heterodimerization.

indirect

PMID: 16979567 Activated TBK1 induces the phosphorylation (P−) of IRF3 and IRF7, resulting in their homo- or heterodimerization.

indirect

PMID: 16979567, 15210742 Inducible IκB kinase (IKKi; also known as IKKε), which is structurally related to TBK1, was also shown to phosphorylate IRF3 and IRF7 in vitro; however, gene-targeting studies revealed that the contribution of IKKi to the cytosolic pathway is minor

PMID: 16979567 Activated TBK1 induces the phosphorylation (P−) of IRF3 and IRF7, resulting in their homo- or heterodimerization. 18) PMID: 16979567 Phosphorylated IRF3 forms homodimers and induces IFN-β and Cxcl10 genes

PMID: 16979567 Activated TBK1 induces the phosphorylation (P−) of IRF3 and IRF7, resulting in their homo- or heterodimerization.

PMID: 16979567 Activated TBK1 induces the phosphorylation (P−) of IRF3 and IRF7, resulting in their homo- or heterodimerization.

PMID: 16979567 These dimers then translocate to the nucleus and induce chemokines (including CXCL10) as well as small amounts of IFN-beta.

PMID: 16979567 These dimers then translocate to the nucleus and induce chemokines (including CXCL10) as well as small amounts of IFN-beta.

PMID: 16979567 These dimers then translocate to the nucleus and induce chemokines (including CXCL10) as well as small amounts of IFN-beta. PMID: 16979567 The activated TBK1 mediates phosphorylation of serine residues in IRF3, rather than those in IRF7, inducing its dimerization and entry into the nucleus where it induces the transcription of the IFN-β gene.

indirect

PMID: 16979567 These dimers then translocate to the nucleus and induce chemokines (including CXCL10) as well as small amounts of IFN-β

indirect

PMID: 16979567 These dimers then translocate to the nucleus and induce chemokines (including CXCL10) as well as small amounts of IFN-β

indirect

PMID: 16979567 These dimers then translocate to the nucleus and induce chemokines (including CXCL10) as well as small amounts of IFN-β 18) PMID: 16979567 Phosphorylated IRF3 forms homodimers and induces IFN-β and Cxcl10 genes

PMID: 16979567 These dimers then translocate to the nucleus and induce chemokines (including CXCL10) as well as small amounts of IFN-β

indirect

PMID: 16979567 These dimers then translocate to the nucleus and induce chemokines (including CXCL10) as well as small amounts of IFN-β

indirect

PMID: 16979567 These dimers then translocate to the nucleus and induce chemokines (including CXCL10) as well as small amounts of IFN-β PMID: 16979567 The activated TBK1 mediates phosphorylation of serine residues in IRF3, rather than those in IRF7, inducing its dimerization and entry into the nucleus where it induces the transcription of the IFN-β gene. PMID: 16979567 In a similar way to the TLR4 signaling, TLR3 activates the Trif- (TRAM is not involved), TBK1-, and IRF3-dependent pathway to induce IFN-β gene

indirect

PMID: 16979567 Secreted IFN-β then stimulates type I IFN receptor (heterodimer of IFNAR1 and IFNAR2) in an autocrine and a paracrine fashion, leading to activation of ISGF3 (heterotrimer of STAT1, STAT2, and IRF9) and the transcription of IRF7 gene.

PMID: 16979567 Secreted IFN-β then stimulates type I IFN receptor (heterodimer of IFNAR1 and IFNAR2) in an autocrine and a paracrine fashion, leading to activation of ISGF3 (heterotrimer of STAT1, STAT2, and IRF9) and the transcription of IRF7 gene.

indirect

PMID: 16979567 Secreted IFN-β then stimulates type I IFN receptor (heterodimer of IFNAR1 and IFNAR2) in an autocrine and a paracrine fashion, leading to activation of ISGF3 (heterotrimer of STAT1, STAT2, and IRF9) and the transcription of IRF7 gene.

indirect

PMID: 16979567 Secreted IFN-β then stimulates type I IFN receptor (heterodimer of IFNAR1 and IFNAR2) in an autocrine and a paracrine fashion, leading to activation of ISGF3 (heterotrimer of STAT1, STAT2, and IRF9) and the transcription of IRF7 gene.

PMID: 16979567,11314014 In addition, other viruses produce proteins that can interact with CBP/p300 and alter their interaction with IRFs, such as the vIRF-1 protein of human herpesvirus 8

PMID: 1679567,9649509,12186937,15664159 Some viruses produce a protein that directly binds to and prevents the transactivation ability of IRF3 or IRF7, including the E6 oncoprotein of the human papillomavirus, the NSP1 of the rotavirus , and the RTA protein of Kaposi's sarcoma-associated herpesvirus

PMID: 1679567,9649509,12186937,15664159 Some viruses produce a protein that directly binds to and prevents the transactivation ability of IRF3 or IRF7, including the E6 oncoprotein of the human papillomavirus, the NSP1 of the rotavirus , and the RTA protein of Kaposi's sarcoma-associated herpesvirus

PMID: 1679567,9649509,12186937,15664159 Some viruses produce a protein that directly binds to and prevents the transactivation ability of IRF3 or IRF7, including the E6 oncoprotein of the human papillomavirus, the NSP1 of the rotavirus , and the RTA protein of Kaposi's sarcoma-associated herpesvirus

PMID: 1679567,9649509,12186937,15664159 Some viruses produce a protein that directly binds to and prevents the transactivation ability of IRF3 or IRF7, including the E6 oncoprotein of the human papillomavirus, the NSP1 of the rotavirus , and the RTA protein of Kaposi's sarcoma-associated herpesvirus

PMID: 1679567,9649509,12186937,15664159 Some viruses produce a protein that directly binds to and prevents the transactivation ability of IRF3 or IRF7, including the E6 oncoprotein of the human papillomavirus, the NSP1 of the rotavirus , and the RTA protein of Kaposi's sarcoma-associated herpesvirus

PMID: 1679567,9649509,12186937,15664159 Some viruses produce a protein that directly binds to and prevents the transactivation ability of IRF3 or IRF7, including the E6 oncoprotein of the human papillomavirus, the NSP1 of the rotavirus , and the RTA protein of Kaposi's sarcoma-associated herpesvirus

indirect

PMID: 1679567,: 16177806 Interestingly, it has been shown that hepatitis C virus (HCV) nonstructural proteins 3 and 4A (NS3/4A) cleave IPS-1, thereby inhibiting the RIG-I- and MDA5-mediated activation of IRF3 and/or IRF7 during HCV infection

PMID: 16979567 TLR4 is the only receptor that can induce type I IFN (IFN-β, not IFN-α) gene by recognizing nonnucleic acid ligands, such as lipopolysaccharide (LPS)

PMID: 16979567, 10359581 TLR4 is expressed on the plasma membrane, and the extracellular portion of TLR4 associates with MD-2, which is prerequisite for TLR4 oligomerization and downstream signaling upon the recognition of LPS

14) PMID: 16979567, 10359581 TLR4 is expressed on the plasma membrane, and the extracellular portion of TLR4 associates with MD-2, which is prerequisite for TLR4 oligomerization and downstream signaling upon the recognition of LPS

pMID: 1679567,15895089 The TLR4-MD-2 complex requires the aid of CD14, a high-affinity receptor for LPS, for the recognition of LPS and subsequent activation of the IFN-β induction pathway

PMID: 1679567,15210742,12872135,14556004 The receptor complex composed of CD14, TLR4, and MD-2 stimulates the signaling pathway through the adaptor proteins TRAM and Trif, which leads to the activation of TBK1

PMID: 1679567,15210742,12872135,14556004 The receptor complex composed of CD14, TLR4, and MD-2 stimulates the signaling pathway through the adaptor proteins TRAM and Trif, which leads to the activation of TBK1

indirect

PMID: 16979567 Trif associates with TBK1 through TRAF3 and NAP1, which mediates the phosphorylation of IRF3. Phosphorylated IRF3 forms homodimers and induces IFN-β and Cxcl10 genes

indirect

17) PMID: 16979567 Trif associates with TBK1 through TRAF3 and NAP1, which mediates the phosphorylation of IRF3. Phosphorylated IRF3 forms homodimers and induces IFN-β and Cxcl10 genes

PMID: 16979567, 11607032,15711573,15558055 TLR3 recognizes poly(I:C) and probably viral dsRNAs derived from dsRNA viruses such as reovirus, or ssRNA viruses such as West Nile virus, respiratory syncytial virus, and EMCV

PMID: 16979567, 11607032,15711573,15558055 TLR3 recognizes poly(I:C) and probably viral dsRNAs derived from dsRNA viruses such as reovirus, or ssRNA viruses such as West Nile virus, respiratory syncytial virus, and EMCV PMID: 16979567, 15961631 Crystallographic studies have shown that TLR3 directly binds to dsRNA and forms a dimer to activate downstream signaling

PMID: 16979567, 15961631 Crystallographic studies have shown that TLR3 directly binds to dsRNA and forms a dimer to activate downstream signaling

PMID: 16979567,15502848 The recognition of dsRNA by TLR3 results in the phosphorylation of two specific tyrosines (Tyr759 and Tyr858) within the cytoplasmic tail of TLR3 and the recruitment of phosphatidylinositol 3-kinase (PI3K) to the receptor

PMID: 16979567, 15502848 The recognition of dsRNA by TLR3 results in the phosphorylation of two specific tyrosines (Tyr759 and Tyr858) within the cytoplasmic tail of TLR3 and the recruitment of phosphatidylinositol 3-kinase (PI3K) to the receptor

indirect

PMID: 16979567 In a similar way to the TLR4 signaling, TLR3 activates the Trif- (TRAM is not involved), TBK1-, and IRF3-dependent pathway to induce IFN-β gene

PMID: 16979567 In a similar way to the TLR4 signaling, TLR3 activates the Trif- (TRAM is not involved), TBK1-, and IRF3-dependent pathway to induce IFN-β gene

indirect

PMID: 16979567 In a similar way to the TLR4 signaling, TLR3 activates the Trif- (TRAM is not involved), TBK1-, and IRF3-dependent pathway to induce IFN-β gene

PMID: 16979567,16858407 It was also reported that the tyrosine kinase c-Src is activated by poly(I:C), associates with TLR3, and is essential for dsRNA-induced IRF3 activation

PMID: 16979567,14530355 It was first shown that TRAF6 interacts with the N-terminal region of Trif through its TRAF domain

PMID: 16979567, 15064760 RIP1 interacts with Trif through the C-terminal RIP homotypic interaction motif (RHIM) of Trif

) PMID: 16979567, 14563635, 12900525 DNA viruses such as herpes simplex virus (HSV) contain many unmethylated CpG motifs in their genome, which are recognized by TLR9 and induce robust type I IFN production in pDCs

PMID: 16979567,14976261,14976262 Likewise, TLR7 signaling is essential for type I IFN induction in response to influenza virus or VSV infection by recognizing viral genomic ssRNA

PMID: 16979567 In contrast to TLR3- or TLR4-mediated Trif-dependent IFN gene induction, the TLR9 subfamily members exclusively utilize MyD88 as the signaling adaptor.

PMID: 16979567,15492225,15361868 MyD88 directly interacts with IRF7 (not with IRF3) through its death domain

PMID: 16979567,15492225, 15361868 IRF7 also interacts with TRAF6, another adaptor molecule functioning downstream of MyD88, and the overexpression of TRAF6 induces type I IFN genes through the activation of IRF7

indirect

PMID: 16979567,15492225, 15361868 IRF7 also interacts with TRAF6, another adaptor molecule functioning downstream of MyD88, and the overexpression of TRAF6 induces type I IFN genes through the activation of IRF7

PMID: 16979567,17018642 Similarly to IRF7, IRF1 directly interacts with MyD88 PMID: 16979567 Thus, the IRF1 induced by IFN-γ binds to MyD88 and is modified by unidentified signaling molecule(s) to migrate into the nucleus and activate gene induction

indirect

indirect

PMID: 16979567 As opposed to IRF7, which is induced by type I IFN, IRF1 is strongly induced by IFN-γ signaling.

PMID: 16979567 Thus, the IRF1 induced by IFN-γ binds to MyD88 and is modified by unidentified signaling molecule(s) to migrate into the nucleus and activate gene induction

indirect

PMID: 16979567 Thus, the IRF1 induced by IFN-γ binds to MyD88 and is modified by unidentified signaling molecule(s) to migrate into the nucleus and activate gene induction

indirect

PMID: 16979567,11961557 Furthermore, IFN-beta gene is induced by several nonviral agents such as the receptor activator of NF-κB ligand (RANKL), which activates NF-κB, c-JUN, and c-Fos, but not IRFs

indirect

PMID: 16979567,11961557 Furthermore, IFN-beta gene is induced by several nonviral agents such as the receptor activator of NF-κB ligand (RANKL), which activates NF-κB, c-JUN, and c-Fos, but not IRFs

indirect

PMID: 16979567,11961557 Furthermore, IFN-beta gene is induced by several nonviral agents such as the receptor activator of NF-κB ligand (RANKL), which activates NF-κB, c-JUN, and c-Fos, but not IRFs

indirect

PMID: 16979567,11961557 Furthermore, IFN-beta gene is induced by several nonviral agents such as the receptor activator of NF-κB ligand (RANKL), which activates NF-κB, c-JUN, and c-Fos, but not IRFs

indirect

PMID: 16979567 Upon TLR7 or TLR9 (expressed in endosomes) stimulation, IRF7 interacting with MyD88 is activated by the IRAK4-IRAK1-IKKalpha kinase cascade.