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z" /> </svg> PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 LR2 recognizes various PAMPs, including peptidoglycan from Gram-positive bacteria, lipoarabinomannan from mycobacteria, hemagglutinin protein from measles virus and tGPI-mutin from Trypanosoma. PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 LR2 recognizes various PAMPs, including peptidoglycan from Gram-positive bacteria, lipoarabinomannan from mycobacteria, hemagglutinin protein from measles virus and tGPI-mutin from Trypanosoma. PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 LR2 recognizes various PAMPs, including peptidoglycan from Gram-positive bacteria, lipoarabinomannan from mycobacteria, hemagglutinin protein from measles virus and tGPI-mutin from Trypanosoma. PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 LR2 recognizes various PAMPs, including peptidoglycan from Gram-positive bacteria, lipoarabinomannan from mycobacteria, hemagglutinin protein from measles virus and tGPI-mutin from Trypanosoma. PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 TLR2/1 and TLR2/6 discriminate the lipid structures between triacyl- and diacyl-lipopeptide, respectively PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 TLR2/1 and TLR2/6 discriminate the lipid structures between triacyl- and diacyl-lipopeptide, respectively PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 TLR2/1 and TLR2/6 discriminate the lipid structures between triacyl- and diacyl-lipopeptide, respectively PMID: 18029230 These microbial components include bacterial lipopolysaccharide (LPS; TLR4 ligand), lipoproteins (TLR2 ligand), flagellin (TLR5 ligand), bacterial CpG DNA (TLR9 ligand), viral single-stranded RNA (TLR7 ligand) and viral double-stranded RNA (TLR3 ligand) PMID: 18029230 TLR4 recognizes bacterial LPS and synthetic MPLA as well as envelope proteins from respiratory syncytial virus (RSV) and mouse mammary tumor virus (MMTV). PMID: 18029230 TLR4 recognizes bacterial LPS and synthetic MPLA as well as envelope proteins from respiratory syncytial virus (RSV) and mouse mammary tumor virus (MMTV). PMID: 18029230 TLR5 detects bacterial flagellin expressed in intestinal epithelial cells as well as CD11c-positive lamina propria in DCs PMID: 18029230 TLR5 detects bacterial flagellin expressed in intestinal epithelial cells as well as CD11c-positive lamina propria in DCs PMID: 18029230 In mice, TLR11 recognizes as yet unknown components of uropathogenic bacteria, and a profilin-like molecule of Toxoplasma gondii. PMID: 18029230 In mice, TLR11 recognizes as yet unknown components of uropathogenic bacteria, and a profilin-like molecule of Toxoplasma gondii. PMID: 18029230 TLR3, 7, 8 and 9, which are localized to endosomes, detect nucleic acids derived from viruses and bacteria. PMID: 18029230 TLR3 recognizes dsRNA, which is produced by many viruses during replication, and poly IC. PMID: 18029230 TLR3, 7, 8 and 9, which are localized to endosomes, detect nucleic acids derived from viruses and bacteria. PMID: 18029230 TLR3 recognizes dsRNA, which is produced by many viruses during replication, and poly IC. PMID: 18029230 TLR7 recognizes ssRNA derived from various viruses and synthetic imidazoquinolines with antitumor properties. PMID: 18029230 TLR7 recognizes ssRNA derived from various viruses and synthetic imidazoquinolines with antitumor properties. PMID:18029230 Human TLR8 also participates in the recognition of ssRNA and imidazoquinolines, whereas the function of mouse TLR8 remains unclear. PMID:18029230 Human TLR8 also participates in the recognition of ssRNA and imidazoquinolines, whereas the function of mouse TLR8 remains unclear. PMID: 18029230 LR9 recognizes CpG DNA motifs present in bacterial and viral genomes as well as non-nucleic acids such as hemozoin from Plasmodium. PMID: 18029230 LR9 recognizes CpG DNA motifs present in bacterial and viral genomes as well as non-nucleic acids such as hemozoin from Plasmodium. PMID: 18029230,17072327 The most frequently activated form of NF-κB in TLR signaling is a heterodimer composed of RelA and p50 PMID: 18029230 Under unstimulated conditions, NF-κB is sequestered in the cytoplasm as an inactive form by interaction with a family of inhibitor proteins known as IκB proteins PMID: 18029230 The RelA–p50 heterodimer is kept in the cytoplasm as a latent and inactive form by interaction with IκB proteins in unstimulated cells PMID: 18029230 Stimulation with TLR ligands triggers the rapid phosphorylation of specific serine residues of IκB proteins by a multiprotein complex termed the IKK complex, which consists of two catalytic components, IKKgreek small letter alpha and IKKβ, and a regulatory component, NEMO (NF-κB essential modifier, also known as IKKγ). indirect PMID: 18029230 Stimulation with TLR ligands triggers the rapid phosphorylation of specific serine residues of IκB proteins by a multiprotein complex termed the IKK complex, which consists of two catalytic components, IKKgreek small letter alpha and IKKβ, and a regulatory component, NEMO (NF-κB essential modifier, also known as IKKγ). PMID: 18029230 Phosphorylated IκB proteins are subsequently polyubiquitinated and degraded by the 26S proteasome, allowing NF-κB to move into the nucleus. indirect PMID: 18029230 Phosphorylated IκB proteins are subsequently polyubiquitinated and degraded by the 26S proteasome, allowing NF-κB to move into the nucleus. PMID: 18029230 Phosphorylated IκB proteins are subsequently polyubiquitinated and degraded by the 26S proteasome, allowing NF-κB to move into the nucleus. indirect PMID: 18029230,17072327 This pathway is called the ‘canonical pathway’ and is responsible for TLR-mediated induction of inflammatory cytokines such as tumor necrosis factor-greek small letter alpha (TNF-greek small letter alpha) and IL-6 PMID: 18029230,17072327 This pathway is called the ‘canonical pathway’ and is responsible for TLR-mediated induction of inflammatory cytokines such as tumor necrosis factor-greek small letter alpha (TNF-greek small letter alpha) and IL-6 PMID: 18029230 TLR4 uses four adaptors, MyD88, TIRAP, TRIF and TRAM. TLR3 uses TRIF as the sole adaptor PMID: 18029230 PMID: 18029230 TLR4 uses four adaptors, MyD88, TIRAP, TRIF and TRAM. TLR3 uses TRIF as the sole adaptor PMID: 18029230 indirect indirect PMID: 18029230,17496917,16858426 TRAF6 is a RING-domain E3 ubiquitin ligase, and together with E2, Ubc13 and Uev1A, it promotes Lys63-linked polyubiquitination of target proteins, including TRAF6 itself and NEMO indirect PMID: 18029230 The activated TAK1 complex then activates the IKK complex consisting of IKKgreek small letter alpha, IKKβ and NEMO, which catalyzes the phosphorylation of IκB proteins (P) indirect PMID: 18029230 Simultaneously, the TAK1 complex activates the MAPK pathway, which results in the phosphorylation (P) and activation of AP-1 PMID: 18029230,17496917 Ubiquitinated NEMO and TRAF6 subsequently recruit a protein kinase complex involving TAK1 (transforming growth factor-β-activated kinase-1) and TABs (TAK1 binding proteins) (TAB1, TAB2 and TAB3), Ubiquitin-mediated activation of TAK1 and IKK, which then activates two distinct pathways involving the IKK complex and the mitogen-activated protein kinase (MAPK) (ERK, JNK, p38) pathway indirect indirect PMID: 18029230 NF-κB and AP-1 control inflammatory responses through the induction of inflammatory cytokines indirect PMID: 18029230 NF-κB and AP-1 control inflammatory responses through the induction of inflammatory cytokines PMID: 18029230 TIRAP and TRAM are required for the activation of the MyD88- and the TRIF-dependent pathways, respectively. PMID: 18029230 TIRAP and TRAM are required for the activation of the MyD88- and the TRIF-dependent pathways, respectively. PMID: 18029230,15064760 he TRIF C-terminal region contains the Rip homotypic interaction motif (RHIM), which is responsible for interaction with RIP1 (receptor-interacting protein-1), a member of the RIP family involved in TNF-receptor-mediated NF-κB activation 29 E. Meylan et al., RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappaB activation PMID: 18029230,16115877 Notably, RIP1 is polyubiquitinated to form a complex with TRAF6 and TAK1, resulting in NF-κB activation PMID:18029230 These findings indicate that TRIF recruits TRAF6 and RIP1 via distinct regions and that these molecules appear to cooperative to facilitate TAK1 activation, resulting in robust NF-κB activation PMID:18029230 These findings indicate that TRIF recruits TRAF6 and RIP1 via distinct regions and that these molecules appear to cooperative to facilitate TAK1 activation, resulting in robust NF-κB activation PMID: 18029230 TLR3 uses TRIF as the sole adaptor. PMID: 18029230 TRIF recruits TRAF3, which then interacts with TBK1 and IKKi. indirect PMID: 18029230 These kinases mediate phosphorylation of IRF3 (P). Phosphorylated IRF3 dimerizes and translocates into the nucleus to regulate transcription PMID: 18029230 These kinases mediate phosphorylation of IRF3 (P). Phosphorylated IRF3 dimerizes and translocates into the nucleus to regulate transcription PMID: 18029230 These kinases mediate phosphorylation of IRF3 (P). Phosphorylated IRF3 dimerizes and translocates into the nucleus to regulate transcription indirect indirect PMID: 18029230 These kinases mediate phosphorylation of IRF3 (P). Phosphorylated IRF3 dimerizes and translocates into the nucleus to regulate transcription PMID: 18029230,16979567 n the nucleus, IRF3 together with NF-κB and ATF2/c-Jun form a multiprotein complex called an enhanceosome, which binds the promoter–enhancer region of the IFN-β gene PMID: 18029230 TBK1 was identified as a protein kinase interacting with TANK (also known as I-TRAF), a TRAF-binding protein PMID: 18029230 TRIF recruits TRAF3, which then interacts with TBK1 and IKKi. PMID: 18029230 This allows IRF3 to form a homodimer, translocate into the nucleus and bind its target sequences, such as IFN-stimulated response element (ISRE). PMID: 18029230 TLR1, 2 and 6 utilize MyD88 and TIRAP as adaptors while TLR5, 7, 9 and 11 utilize MyD88. PMID: 18029230 In pDCs, IRF7 forms a signaling complex with MyD88, IRAK4, TRAF6, IRAK1 and IKKalpha PMID: 18029230 IRAK1, but not IRAK4, physically interacts with IRF7 PMID: 18029230 TRAF3 binds to a MyD88–IRAK1–IRF7 complex and pDCs derived from TRAF3-deficient mice have defects in IFN-greek small letter alpha production PMID: 18029230 In response to ligand stimulation, IRF7 is phosphorylated by IRAK1 and IKKalpha PMID: 18029230 n response to ligand stimulation, IRF7 is phosphorylated by IRAK1 and IKKgreek small letter alpha, dimerizes and is then translocated into the nucleus. PMID: 18029230 n response to ligand stimulation, IRF7 is phosphorylated by IRAK1 and IKKgreek small letter alpha, dimerizes and is then translocated into the nucleus. PMID: 18029230 IRF7 regulates the expression of type I IFNs, including IFN-greek small letter alpha and IFN-β PMID: 18029230 IRF7 regulates the expression of type I IFNs, including IFN-greek small letter alpha and IFN-β PMID: 18029230 TLR1, 2 and 6 utilize MyD88 and TIRAP as adaptors PMID: 18029230 TLR1, 2 and 6 utilize MyD88 and TIRAP as adaptors PMID: 18029230 MyD88 recruits TRAF6 and members of the IRAK family PMID: 18029230,15229469 Upon TLR activation, through its death domain, MyD88 interacts with the death domains of members of the IRAK (IL-1 receptor-associated kinase) family of protein kinases, including IRAK1, IRAK2, IRAK4 and IRAK-M, PMID: 18029230 IRAK4 is initially activated, which in turn phosphorylates and activates IRAK1. PMID: 18029230 MyD88 recruits TRAF6 and members of the IRAK family PMID: 18029230,15229469 Upon TLR activation, through its death domain, MyD88 interacts with the death domains of members of the IRAK (IL-1 receptor-associated kinase) family of protein kinases, including IRAK1, IRAK2, IRAK4 and IRAK-M, PMID: 18029230 IRAK4 is initially activated, which in turn phosphorylates and activates IRAK1. PMID: 18029230 After IRAK4 and IRAK1 have been sequentially phosphorylated, they dissociate from MyD88 and interact with TRAF6. PMID: 18029230 After IRAK4 and IRAK1 have been sequentially phosphorylated, they dissociate from MyD88 and interact with TRAF6. PMID: 18029230,17496917,16858426 TRAF6 is a RING-domain E3 ubiquitin ligase, and together with E2, Ubc13 and Uev1A, it promotes Lys63-linked polyubiquitination of target proteins, including TRAF6 itself and NEMO PMID: 18029230 MyD88 recruits TRAF6 and members of the IRAK family PMID: 18029230,15229469 Upon TLR activation, through its death domain, MyD88 interacts with the death domains of members of the IRAK (IL-1 receptor-associated kinase) family of protein kinases, including IRAK1, IRAK2, IRAK4 and IRAK-M, PMID: 18029230 IRAK4 is initially activated, which in turn phosphorylates and activates IRAK1. PMID: 18029230 MyD88 recruits TRAF6 and members of the IRAK family PMID: 18029230,15229469 Upon TLR activation, through its death domain, MyD88 interacts with the death domains of members of the IRAK (IL-1 receptor-associated kinase) family of protein kinases, including IRAK1, IRAK2, IRAK4 and IRAK-M, PMID: 18029230 IRAK4 is initially activated, which in turn phosphorylates and activates IRAK1. PMID: 18029230 After IRAK4 and IRAK1 have been sequentially phosphorylated, they dissociate from MyD88 and interact with TRAF6. PMID: 18029230 Pretreatment of MyD88-deficient cells with cyclohexamide, a protein synthesis inhibitor, results in an abrogation of LPS-induced NF-κB activation, thus suggesting that late phase NF-κB activation is likely to require protein synthesis. PMID: 18029230 LPS induces TNF-greek small letter alpha synthesis via a MyD88-independent mechanism, and the newly synthesized TNF-greek small letter alpha subsequently binds TNF receptor to initiate the late phase NF-κB activation in an autocrine manner, at least in MEF cells. indirect PMID: 18029230 LPS induces TNF-greek small letter alpha synthesis via a MyD88-independent mechanism, and the newly synthesized TNF-greek small letter alpha subsequently binds TNF receptor to initiate the late phase NF-κB activation in an autocrine manner, at least in MEF cells. PMID: 18029230 LPS induces TNF-greek small letter alpha synthesis via a MyD88-independent mechanism, and the newly synthesized TNF-greek small letter alpha subsequently binds TNF receptor to initiate the late phase NF-κB activation in an autocrine manner, at least in MEF cells. PMID: 18029230 RIG-I and Mda5 contain CARD-like structures that mediate interaction with the adaptor IPS-1 PMID: 18029230 RIG-I and Mda5 contain CARD-like structures that mediate interaction with the adaptor IPS-1 PMID: 18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi–IRF3/7 axis PMID: 18029230,16585540 In parallel, IPS-1 interacts with FADD and caspase-8/-10, causing NF-κB activation PMID: 18029230,17468758 NEMO is shown to participate in both NF-κB and IRF3 activation in RIG-I and Mda5 signaling pathways PMID: 18029230 Cells express cytoplasmic RNA helicases (RIG-I and Mda5) that recognize RNA derived from actively replicating RNA viruses. PMID: 18029230 Cells express cytoplasmic RNA helicases (RIG-I and Mda5) that recognize RNA derived from actively replicating RNA viruses. PMID: 18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi–IRF3/7 axis PMID: 18029230,16585540 In parallel, IPS-1 interacts with FADD and caspase-8/-10, causing NF-κB activation PMID: 18029230,17468758 NEMO is shown to participate in both NF-κB and IRF3 activation in RIG-I and Mda5 signaling pathways indirect PMID:18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi–IRF3/7 axis indirect PMID:18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi–IRF3/7 axis PMID: 18029230,16585540 In parallel, IPS-1 interacts with FADD and caspase-8/-10, causing NF-κB activation indirect PMID: 18029230,16585540 In parallel, IPS-1 interacts with FADD and caspase-8/-10, causing NF-κB activation indirect PMID: 18029230 IKKi can phosphorylate a serine residue in STAT1 that is crucial for the transcriptional activity PMID: 18029230,17618271 Recently, DAI (DNA-dependent activator of interferon-regulatory factors, also known as DLM-1 and ZBP1) has been identified as a cytosolic sensor for dsDN PMID: 18029230 DAI is an IFN-inducible gene that has dsDNA-binding properties PMID: 18029230 Whereas DAI activates IRF3 via direct interactions with TBK1 and IRF3, pathways for NF-κB activation remain unknown. PMID: 18029230 Whereas DAI activates IRF3 via direct interactions with TBK1 and IRF3, pathways for NF-κB activation remain unknown. indirect PMID:18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi–IRF3/7 axis PMID:18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi–IRF3/7 PMID: 18029230,12702806 TBK1 and IKKi can also phosphorylate and activate IRF7, which is the member of IRF family most closely related to IRF3 PMID: 18029230 IPS-1 interacts with TRAF3, which subsequently activates the TBK1/IKKi–IRF3/7 axis indirect PMID: 18029230 Ubiquitin-dependent proteolytic degradation of the C-terminal region of p105 and p100 results in the generation of mature p50 and p52 PMID: 18029230 Ubiquitin-dependent proteolytic degradation of the C-terminal region of p105 and p100 results in the generation of mature p50 and p52 PMID: 18029230 Importantly, p100 phosphorylation is mediated by the IKKgreek small letter alpha–IKKgreek small letter alpha homodimer, which does not require IKKbeta and NEMO. indirect PMID: 18029230 p52 then forms a heterodimer with RelB to regulate expression of target genes. indirect PMID: 18029230 p52 then forms a heterodimer with RelB to regulate expression of target genes. PMID: 18029230,11460167 It has been suggested that TAK1 can phosphorylate IKKβ and increase its enzymatic activity PMID: 18029230,17496917 Ubiquitinated NEMO and TRAF6 subsequently recruit a protein kinase complex involving TAK1 (transforming growth factor-β-activated kinase-1) and TABs (TAK1 binding proteins) (TAB1, TAB2 and TAB3), Ubiquitin-mediated activation of TAK1 and IKK, which then activates two distinct pathways involving the IKK complex and the mitogen-activated protein kinase (MAPK) (ERK, JNK, p38) pathway PMID: 18029230,17496917 Ubiquitinated NEMO and TRAF6 subsequently recruit a protein kinase complex involving TAK1 (transforming growth factor-β-activated kinase-1) and TABs (TAK1 binding proteins) (TAB1, TAB2 and TAB3), Ubiquitin-mediated activation of TAK1 and IKK, which then activates two distinct pathways involving the IKK complex and the mitogen-activated protein kinase (MAPK) (ERK, JNK, p38) pathway indirect PMID: 18029230,17496917 Ubiquitinated NEMO and TRAF6 subsequently recruit a protein kinase complex involving TAK1 (transforming growth factor-β-activated kinase-1) and TABs (TAK1 binding proteins) (TAB1, TAB2 and TAB3), Ubiquitin-mediated activation of TAK1 and IKK, which then activates two distinct pathways involving the IKK complex and the mitogen-activated protein kinase (MAPK) (ERK, JNK, p38) pathway indirect PMID: 18029230,17496917 Ubiquitinated NEMO and TRAF6 subsequently recruit a protein kinase complex involving TAK1 (transforming growth factor-β-activated kinase-1) and TABs (TAK1 binding proteins) (TAB1, TAB2 and TAB3), Ubiquitin-mediated activation of TAK1 and IKK, which then activates two distinct pathways involving the IKK complex and the mitogen-activated protein kinase (MAPK) (ERK, JNK, p38) pathway PMID: 18029230,16115877 Notably, RIP1 is polyubiquitinated to form a complex with TRAF6 and TAK1, resulting in NF-κB activation indirect PMID: 18029230,16115877 Notably, RIP1 is polyubiquitinated to form a complex with TRAF6 and TAK1, resulting in NF-κB activation PMID: 18029230 t has been shown that NAK enhances the enzymatic activity of IKKβ through direct phosphorylation, contributing to NF-κB activation. PMID: 18029230,15064760 he TRIF C-terminal region contains the Rip homotypic interaction motif (RHIM), which is responsible for interaction with RIP1 (receptor-interacting protein-1), a member of the RIP family involved in TNF-receptor-mediated NF-κB activation 29 E. Meylan et al., RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappaB activation