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PMID: 16410796 TLR1/2 and TLR2/6 discriminate triacyl lipopeptide and diacyl lipopeptide, respectively.

PMID: 16410796 TLR1/2 and TLR2/6 discriminate triacyl lipopeptide and diacyl lipopeptide, respectively.

PMID: 16410796 TLR1/2 and TLR2/6 discriminate triacyl lipopeptide and diacyl lipopeptide, respectively.

PMID: 16410796 TLR1/2 and TLR2/6 discriminate triacyl lipopeptide and diacyl lipopeptide, respectively.

PMID: 16410796, 11607032 TLR3 recognizes double-stranded RNA (dsRNA) that is produced from many viruses during replication.

PMID: 16410796, 11323673 TLR5 recognizes bacterial flagellin.

PMID: 16410796, 11812998, 14976261, 14976262, 14579267, 12032557, 15034168, 15723075 TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, single-stranded RNA (ssRNA) derived from human immunodeficiency virus type I (HIV-1), vesicular stomatitis virus (VSV) and influenza virus, and certain siRNAs.

PMID: 16410796, 11812998, 14976261, 14976262, 14579267, 12032557, 15034168, 15723075 TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, single-stranded RNA (ssRNA) derived from human immunodeficiency virus type I (HIV-1), vesicular stomatitis virus (VSV) and influenza virus, and certain siRNAs.

PMID: 16410796, 14976262, 14579267, 12032557 human TLR8 mediates the recognition of imidazoquinolines and ssRNA.

PMID: 16410796, 14976262, 14579267, 12032557 human TLR8 mediates the recognition of imidazoquinolines and ssRNA.

PMID: 16410796, 11130078, 15345224, 12900525, 15630134 TLR9 recognizes bacterial and viral CpG DNA motifs and malaria pigment hemozoin.

PMID: 16410796, 11130078, 15345224, 12900525, 15630134 TLR9 recognizes bacterial and viral CpG DNA motifs and malaria pigment hemozoin.

PMID: 16410796, 9851930, 10201887 LPS of Gram-negative bacteria is recognized by TLR4 (hToll)

PMID: 16410796 Upon stimulation with various TLR ligands, IkappaBs are phosphorylated at serine residues by an IKK complex.

PMID: 16410796 The phosphorylation targets IkappaBs for ubiquitination and degradation by the 26S proteasome, allowing NF-kappaB to be released into the nucleus and to bind to the kappaB site.

PMID: 16410796 The phosphorylation targets IkappaBs for ubiquitination and degradation by the 26S proteasome, allowing NF-kappaB to be released into the nucleus and to bind to the kappaB site.

PMID: 16410796 The phosphorylation targets IkappaBs for ubiquitination and degradation by the 26S proteasome, allowing NF-kappaB to be released into the nucleus and to bind to the kappaB site.

PMID: 16410796 TIRAP/Mal and TRAM are required for the activation of MyD88- and Trif-dependent pathways, respectively.

PMID: 16410796 MyD88 is a central adapter shared by almost all TLRs. The association of TLRs and MyD88 recruits members of the interleukin-1 receptor-associated kinase (IRAK) family.

PMID: 16410796 The association of TLRs and MyD88 recruits members of the interleukin-1 receptor-associated kinase (IRAK) family.

PMID: 16410796 In response to stimuli, IRAK4 and IRAK1 are sequentially phosphorylated and dissociated from MyD88.

PMID: 16410796 In response to stimuli, IRAK4 and IRAK1 are sequentially phosphorylated and dissociated from MyD88.

indirect

PMID: 16410796, 14556004 TRAM is required for the activation of the Trif-dependent pathway, indicating that TRAM is an adapter linking TLR4 to Trif.

PMID: 16410796, 16056267 TRAF6 which contains an N-terminal RING domain that is found in a number of E3 ubiquitin ligases, and forms a complex with Ubc13 and Uev1A, serving as the ubiquitin E3 ligase to promote synthesis of lysine 63-linked polyubiquitin chains.

PMID: 16410796, 16056267 TRAF6 in turn activates transforming growth factor-beta-activated protein kinase 1 (TAK1), a member of the MAP kinase kinase kinase (MAP3K) family, in a ubiquitin-dependent manner.

indirect

PMID: 16410796 TAK1 activates the IKK complex that leads to NF-kappaB activation.

PMID: 16410796 TAK1 forms a complex with TAB1, TAB2 and TAB3.

PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.

PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.

indirect

PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.

indirect

PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.

indirect

PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.

indirect

PMID: 16410796 TAK1 simultaneously phosphorylates two members of the MAP kinase kinase family, MKK3 and MKK6, which subsequently activate JNK and p38.

indirect

PMID: 16410796 ERK is also activated in response to TLR ligands through the activation of MEK1 and MEK2, although an upstream kinase activating MEK1 and MEK2 in TLR signaling remains unknown.

indirect

PMID: 16410796 ERK is also activated in response to TLR ligands through the activation of MEK1 and MEK2, although an upstream kinase activating MEK1 and MEK2 in TLR signaling remains unknown.

PMID: 16410796 AP-1 activation in TLR signaling is mostly mediated by MAP kinases such as c-Jun N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK). PMID: 16410796 TAK1 simultaneously activates the MAP kinase pathway, which results in phosphorylation (P) and activation of AP-1.

PMID: 16410796 AP-1 activation in TLR signaling is mostly mediated by MAP kinases such as c-Jun N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK). PMID: 16410796 TAK1 simultaneously activates the MAP kinase pathway, which results in phosphorylation (P) and activation of AP-1.

PMID: 16410796 AP-1 activation in TLR signaling is mostly mediated by MAP kinases such as c-Jun N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK). PMID: 16410796 TAK1 simultaneously activates the MAP kinase pathway, which results in phosphorylation (P) and activation of AP-1.

PMID: 16410796 Trif is the sole adapter utilized by TLR3.

PMID: 16410796, 14556004 TRAM is required for the activation of the Trif-dependent pathway, indicating that TRAM is an adapter linking TLR4 to Trif.

PMID: 16410796, 15064760 Trif–RIP1 interactions are responsible for NF-kappaB activation in TLR3 signaling.

indirect

PMID: 16410796, 15064760 Trif–RIP1 interactions are responsible for NF-kappaB activation in TLR3 signaling.

PMID: 16410796 Trif possesses three typical TRAF6-binding domains in the N-terminal region, which mediate interaction with TRAF6.

indirect

PMID: 16410796 Trif activates NF-kappaB by recruiting TRAF6.

PMID: 16410796 TLR4 also recruits TRAM and Trif, which interacts with TBK1.

PMID: 16410796 TBK1 together with IKKi mediates phosphorylation of IRF3.

PMID: 16410796 TBK1 together with IKKi mediates phosphorylation of IRF3.

PMID: 16410796 Phosphorylated IRF3 is dimerized and translocated into nucleus to bind DNA.

PMID: 16410796 Phosphorylated IRF3 is dimerized and translocated into nucleus to bind DNA.

PMID: 16410796 Initial induction of IFNbeta is largely dependent on IRF3 activation.

PMID: 16410796 After ligand ligation, these TLRs elicit the MyD88-dependent pathway to regulate inflammatory responses by activating NF-kappaB and AP-1.

PMID: 16410796 In pDCs, IRF7 is constitutively expressed and forms a signaling complex with MyD88, IRAK1 and IRAK4.

PMID: 16410796 In response to ligand stimulation, IRF7 is phosphorylated by IRAK1, dimerized and translocated into nuclei.

PMID: 16410796 In response to ligand stimulation, IRF7 is phosphorylated by IRAK1, dimerized and translocated into nuclei. Additionally, TRAF6-dependent ubiquitination is also required for IRF7 activation.

PMID: 16410796 In response to ligand stimulation, IRF7 is phosphorylated by IRAK1, dimerized and translocated into nuclei.

PMID: 16410796 In response to ligand stimulation, IRF7 is phosphorylated by IRAK1, dimerized and translocated into nuclei.

PMID: 16410796, 15665823 It is also reported that IRF5 interacts with MyD88.

indirect

PMID: 16410796 IRF5 translocates into the nucleus in response to ligand stimulation.

PMID: 16410796, 15210742, 15556946 Although it is reported that IRF5 is phosphorylated by TBK1 and IKKi in vitro, cells deficient in TBK1 and IKKi show normal inflammatory responses in response to various TLR ligands.

PMID: 16410796, 15210742, 15556946 Although it is reported that IRF5 is phosphorylated by TBK1 and IKKi in vitro, cells deficient in TBK1 and IKKi show normal inflammatory responses in response to various TLR ligands.

PMID: 16410796 The helicase domain of RIG-I interacts with dsRNA.

PMID: 16410796, 16116171 LGP2 is also related to RIG-I and Mda5, but lacks the CARD-like domains, and is therefore suggested to function as a negative regulator for RIG-I and Mda5.

PMID: 16410796, 11805321, 12015121, 15563593 Melanoma differentiation-associated gene 5 (Mda5) (also known as Helicard) is structurally similar to RIG-I, which also contains two CARD-like and a single helicase domain, and is suggested to mediate antiviral responses.

PMID: 16410796 IPS-1 interacts with RIG-I and Mda5 via the CARD domain.

PMID: 16410796 IPS-1 interacts with RIG-I and Mda5 via the CARD domain.

PMID: 16410796, 16127453 IPS-1 interacts with FADD and RIP-1 via non-CARD region to facilitate NF-kappaB, rather than IRF3 activation.

PMID: 16410796, 16153868 VISA contains two TRAF6-binding domains, and interacts with TRAF6 through these domains.

indirect

PMID: 16410796, 16153868 VISA–TRAF6 interaction is required for NF-kappaB but not IRF3 activation.

PMID: 16410796, 16153868 VISA interacts with Trif.

indirect

PMID: 16410796 IPS-1 initiates intracellular signaling pathways leading to IRF3, NF-kappaB and AP-1 via TBK1/IKKi, IKKalpha/IKKbeta and MAP kinases, respectively.

PMID: 16410796 IPS-1 initiates intracellular signaling pathways leading to IRF3, NF-kappaB and AP-1 via TBK1/IKKi, IKKalpha/IKKbeta and MAP kinases, respectively.