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PMID: 16930560 LPS was known to be concentrated from the plasma by LPS binding protein (LBP), and CD14 was identified as a receptor for LPS on the surface of the cells

PMID: 16930560 The other antibacterial TLRs are TLR2, which in combination with TLR1 recognises triacylated lipopeptides, or in combination with TLR6 recognises diacylated lipopeptides; and TLR5 which recognises bacterial flagellin.

PMID: 16930560 The other antibacterial TLRs are TLR2, which in combination with TLR1 recognises triacylated lipopeptides, or in combination with TLR6 recognises diacylated lipopeptides; and TLR5 which recognises bacterial flagellin.

PMID: 16930560 The other antibacterial TLRs are TLR2, which in combination with TLR1 recognises triacylated lipopeptides, or in combination with TLR6 recognises diacylated lipopeptides; and TLR5 which recognises bacterial flagellin.

PMID: 16930560 The other antibacterial TLRs are TLR2, which in combination with TLR1 recognises triacylated lipopeptides, or in combination with TLR6 recognises diacylated lipopeptides; and TLR5 which recognises bacterial flagellin.

PMID: 16930560 The other antibacterial TLRs are TLR2, which in combination with TLR1 recognises triacylated lipopeptides, or in combination with TLR6 recognises diacylated lipopeptides; and TLR5 which recognises bacterial flagellin.

PMID: 16930560 The anti-viral TLRs are TLR3 which recognises double stranded RNA, TLR7 and TLR8 which bothrecognise single strandedRNA,andTLR9which recognises CpGmotifs, that exist in both virus and bacteria

PMID: 16930560 The anti-viral TLRs are TLR3 which recognises double stranded RNA, TLR7 and TLR8 which bothrecognise single strandedRNA,andTLR9which recognises CpGmotifs, that exist in both virus and bacteria

PMID: 16930560 The anti-viral TLRs are TLR3 which recognises double stranded RNA, TLR7 and TLR8 which bothrecognise single strandedRNA,andTLR9which recognises CpGmotifs, that exist in both virus and bacteria

PMID: 16930560 The anti-viral TLRs are TLR3 which recognises double stranded RNA, TLR7 and TLR8 which bothrecognise single strandedRNA,andTLR9which recognises CpGmotifs, that exist in both virus and bacteria

PMID: 16930560 Finally various fungal and protozoal products are sensed by TLR2.

PMID: 16930560 As is now well known, NFkB is regulated by an inhibitory molecule called inhibitory kB (IkB) which retains NFkB in the cytoplasm under normal conditions.

PMID: 16930560 On TLR ligation, TLR4 dimers and TLR2 heterodimerised with TLR1 or TLR6 recruit Mal and MyD88 to their TIR domains, TLR7/8/9 recruit MyD88 alone.

PMID: 16930560 On TLR ligation, TLR4 dimers and TLR2 heterodimerised with TLR1 or TLR6 recruit Mal and MyD88 to their TIR domains, TLR7/8/9 recruit MyD88 alone. PMID: 16930560 MyD88, which has a C-terminal TIR domain, and an N-terminal death domain associates with the TIR domain of the TLRs and upon binding of ligand to the receptor MyD88 recruits IRAK4 to the TLR receptor complex through the interaction of the death domains of both molecules and facilitates IRAK-4-mediated phosphorylation of IRAK-1.

PMID: 16930560 MyD88, which has a C-terminal TIR domain, and an N-terminal death domain associates with the TIR domain of the TLRs and upon binding of ligand to the receptor MyD88 recruits IRAK4 to the TLR receptor complex through the interaction of the death domains of both molecules and facilitates IRAK-4-mediated phosphorylation of IRAK-1.

PMID: 16930560 The presence of IRAK-4 is required for the recruitment of IRAK-1 to the receptor complex and for the activation and subsequent degradation of IRAK-1 protein.

PMID: 16930560 MyD88, which has a C-terminal TIR domain, and an N-terminal death domain associates with the TIR domain of the TLRs and upon binding of ligand to the receptor MyD88 recruits IRAK4 to the TLR receptor complex through the interaction of the death domains of both molecules and facilitates IRAK-4-mediated phosphorylation of IRAK-1.

PMID: 16930560,11960013,8837778,11923871 Phosphorylated IRAK-1 subsequently dissociates from the receptor complex and associates with TRAF6

PMID: 16930560,11960013,8837778,11923871 Phosphorylated IRAK-1 subsequently dissociates from the receptor complex and associates with TRAF6

PMID: 16930560 IRAK1 binds TRAF6 which in turn binds a pre-formed membrane bound complex of TAB1/ TAK1/TAB2. PMID: 16930560 TRAF6 and IRAK1 then dissociate from the receptor complex and interact with a membrane bound pre-associated complex of TGF-b activated kinase (TAK1) and two TAK1-binding proteins (TAB), termed TAB1 and TAB2

PMID: 16930560 IRAK1 binds TRAF6 which in turn binds a pre-formed membrane bound complex of TAB1/ TAK1/TAB2. PMID: 16930560 TRAF6 and IRAK1 then dissociate from the receptor complex and interact with a membrane bound pre-associated complex of TGF-b activated kinase (TAK1) and two TAK1-binding proteins (TAB), termed TAB1 and TAB2

PMID: 16930560,11460167,11518704,12242293 Ubiquitination of TRAF6 and TAK1 activate the complex, and phosphorylation of TAK1 and TAB2 initiates the release of the complex from the membrane PMID: 16930560 A series of ubiquitination reactions then occur on TRAF6 itself and on its substrate TAK1.

PMID: 16930560,11518704,12242293 Phosphorylation of TAK1 and TAB2 occurs initiating the dissociation of TRAF6/TAK1/TAB1/TAB2 from the membrane to the cytosol, and IRAK-1 degradation PMID: 16930560,11460167,11518704,12242293 Ubiquitination of TRAF6 and TAK1 activate the complex, and phosphorylation of TAK1 and TAB2 initiates the release of the complex from the membrane

PMID: 16930560,11518704,12242293 Phosphorylation of TAK1 and TAB2 occurs initiating the dissociation of TRAF6/TAK1/TAB1/TAB2 from the membrane to the cytosol, and IRAK-1 degradation PMID: 16930560,11460167,11518704,12242293 Ubiquitination of TRAF6 and TAK1 activate the complex, and phosphorylation of TAK1 and TAB2 initiates the release of the complex from the membrane

indirect

PMID: 16930560,9346484 Active TAK1 phosphorylates the IKK complex, which in turn phosphorylates IkB targeting IkB for degradation PMID: 16930560 TAK1 is subsequently active and can then phosphorylate downstream targets such as the IkB kinases (IKKs).

PMID: 16930560 TRIF binds to TLR3 and recruits TRAF6 directly through a TRAF6-binding motif in its N-terminal domain.

PMID: 16930560 TRIF binds to TLR3 and recruits TRAF6 directly through a TRAF6-binding motif in its N-terminal domain.

indirect

PMID: 16930560,14530355,12609980,14982987 TRIF binds to TLR3 and recruits TRAF6 directly through a TRAF6-binding motif in its N-terminal domain. This leads to TAK1 activation and subsequent NFkB activation in an IRAK1 and IRAK4 independent manner

PMID: 16930560,15064760 The C-terminal of TRIF possesses a RIP homotypic interaction motif (RHIM), and it associates with receptor interacting protein 1 (RIP1) through homophilic interaction of RHIM domains. PMID: 16930560,15064760 TRIF also binds directly to RIP1 which binds TRAF6 and leads to the activation of the IKK complex

PMID: 16930560,15064760 TRIF also binds directly to RIP1 which binds TRAF6 and leads to the activation of the IKK complex

indirect

PMID: 16930560,15064760 TRIF also binds directly to RIP1 which binds TRAF6 and leads to the activation of the IKK complex

PMID: 16930560 Btk interacts with the TIR domain of TLR4 PMID: 16930560 More recently it has been found that Btk interacts with the TIR domains of many of the TLRs including that of TLR4 and also with Mal and MyD88, the adapters used by TLR4

PMID: 16930560 On TLR ligation, TLR4 dimers and TLR2 heterodimerised with TLR1 or TLR6 recruit Mal and MyD88 to their TIR domains, TLR7/8/9 recruit MyD88 alone.

PMID: 16930560 LPS induces tyrosine phosphorylation of Btk and activates its kinase activity.

PMID: 16930560,15081522,12724322,15849198,16439361 It has since been shown that Btk directly phosphorylates Mal and functions on the pathway from TLR4 to the phosphorylation of the p65 subunit of NFkB, promoting transactivation

PMID: 16930560,10837071,9346484,9244310,9346485,9346241 Once activated the IKK complex induces phosphorylation and subsequent degradation of IkB, which leads to the translocation of NFkB culminating in NFkB activation and the expression of pro-inflammatory cytokines

PMID: 16930560,8011280 Once activated by a PAMP, a TLR triggers a cascade of cellular signals, culminating in the eventual activationofNFkBwhichbinds to a discretenucleotide sequence in the upstream regions of genes that produce proinflammatory cytokines, such as TNFa, IL-1, and IL-2, thereby regulating their expression PMID: 16930560 As NFkB is a key transcription factor regulating the expression of IL-1b and TNFa they examined the ability of LPS to induce expression of Rel-family proteins.

indirect

PMID: 16930560,8011280 Once activated by a PAMP, a TLR triggers a cascade of cellular signals, culminating in the eventual activationofNFkBwhichbinds to a discretenucleotide sequence in the upstream regions of genes that produce proinflammatory cytokines, such as TNFa, IL-1, and IL-2, thereby regulating their expression

indirect

PMID: 16930560,8011280 Once activated by a PAMP, a TLR triggers a cascade of cellular signals, culminating in the eventual activationofNFkBwhichbinds to a discretenucleotide sequence in the upstream regions of genes that produce proinflammatory cytokines, such as TNFa, IL-1, and IL-2, thereby regulating their expression

indirect

PMID: 16930560,8011280 Once activated by a PAMP, a TLR triggers a cascade of cellular signals, culminating in the eventual activationofNFkBwhichbinds to a discretenucleotide sequence in the upstream regions of genes that produce proinflammatory cytokines, such as TNFa, IL-1, and IL-2, thereby regulating their expression PMID:16930560,16166516,16166517 TNFa expression is induced in an NFkB-independent IRF3-dependent manner, binds to the TNF receptor and induces NFkB activation providing delayed NFkB induction

indirect

PMID: 16930560,8011280 Once activated by a PAMP, a TLR triggers a cascade of cellular signals, culminating in the eventual activationofNFkBwhichbinds to a discretenucleotide sequence in the upstream regions of genes that produce proinflammatory cytokines, such as TNFa, IL-1, and IL-2, thereby regulating their expression

indirect

PMID: 16930560,8011280 Once activated by a PAMP, a TLR triggers a cascade of cellular signals, culminating in the eventual activationofNFkBwhichbinds to a discretenucleotide sequence in the upstream regions of genes that produce proinflammatory cytokines, such as TNFa, IL-1, and IL-2, thereby regulating their expression

indirect

indirect

PMID: 16930560 At this point in time the ligands for TLRs were unknown and researchers only knew that by constitutively activating TLRs they could drive NFkB activation and cause the production of the proinflammatory cytokines TNFa, IL-1, IL-6 and IL-8.

indirect

indirect

PMID: 16930560 At this point in time the ligands for TLRs were unknown and researchers only knew that by constitutively activating TLRs they could drive NFkB activation and cause the production of the proinflammatory cytokines TNFa, IL-1, IL-6 and IL-8.

PMID: 16930560 LPS was known to be concentrated from the plasma by LPS binding protein (LBP), and CD14 was identified as a receptor for LPS on the surface of the cells

PMID: 16930560 The best characterised is TLR4, which recognises the Gram-negative product lipopolysaccharide (LPS).

indirect

PMID: 16930560,10837071,9346484,9244310,9346485,9346241 Once activated the IKK complex induces phosphorylation and subsequent degradation of IkB, which leads to the translocation of NFkB culminating in NFkB activation and the expression of pro-inflammatory cytokines

PMID: 16930560,10837071,9346484,9244310,9346485,9346241 Once activated the IKK complex induces phosphorylation and subsequent degradation of IkB, which leads to the translocation of NFkB culminating in NFkB activation and the expression of pro-inflammatory cytokines

indirect

indirect

PMID; 16930560,8258685 Soon afterwards it was reported that PTKs were required for the induction of the pro-inflammatory cytokines IL-1b, IL-6 and TNFa in response to LPS in murine macrophages

indirect

indirect

PMID; 16930560,8258685 Soon afterwards it was reported that PTKs were required for the induction of the pro-inflammatory cytokines IL-1b, IL-6 and TNFa in response to LPS in murine macrophages

indirect

indirect

PMID; 16930560,8258685 Soon afterwards it was reported that PTKs were required for the induction of the pro-inflammatory cytokines IL-1b, IL-6 and TNFa in response to LPS in murine macrophages

indirect

PMID: 16930560 As NFkB is a key transcription factor regulating the expression of IL-1b and TNFa they examined the ability of LPS to induce expression of Rel-family proteins.

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PMID: 16930560 To date, five distinct serine residues have been identified on the p65 NFkB subunit that are inducibly phosphorylated in response to LPS, TNFa, and IL-1.

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PMID: 16930560 To date, five distinct serine residues have been identified on the p65 NFkB subunit that are inducibly phosphorylated in response to LPS, TNFa, and IL-1.

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PMID: 16930560 To date, five distinct serine residues have been identified on the p65 NFkB subunit that are inducibly phosphorylated in response to LPS, TNFa, and IL-1. PMID: 16930560,9660950,9150141 Serine 276 in the RHD on p65 is phosphorylated by protein kinase A (PKA) in response to LPS

PMID: 16930560,11931769,9660950 Zhong et al. found that LPS stimulated PKAdependent phosphorylation of p65 on serine 276 promotes its interaction with the coactivator CREB-binding protein (CBP), potentiating NFkB transcription

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PMID: 16930560 They found that IKKb plays an essential role in LPS-induced serine 536 phosphorylation in MEFs,while IKKa is only partially required for serine 536 phosphorylation

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PMID: 16930560 They found that IKKb plays an essential role in LPS-induced serine 536 phosphorylation in MEFs,while IKKa is only partially required for serine 536 phosphorylation

PMID: 16930560,11356851 A new nuclear IkB protein, IkBz, arrived on the scene relatively recently, which has been shown to interact with NFkB via a Cterminal ankyrin repeat domain in the nucleus

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PMID: 16930560 IkBz is barely detectable in resting cells but it is dramatically induced in response to TLR ligands such as LPS, lipopeptides and CpG DNA, in a MyD88 dependent manner.

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PMID: 16930560 IkBz is barely detectable in resting cells but it is dramatically induced in response to TLR ligands such as LPS, lipopeptides and CpG DNA, in a MyD88 dependent manner.

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PMID:16930560 IkBz is essential for the induction of a subset of inflammatory genes including IL-6 and the IL-12p40 subunit.

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PMID:16930560 IkBz is essential for the induction of a subset of inflammatory genes including IL-6 and the IL-12p40 subunit.

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PMID: 16930560,15618216 Interestingly overexpression of IkBz results in an augmentation of IL-6 production in response to LPS, but inhibits TNFa production

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PMID: 16930560,15618216 Interestingly overexpression of IkBz results in an augmentation of IL-6 production in response to LPS, but inhibits TNFa production

PMID: 16930560,14517278 TLR3 recruits TRIF to its TIR domain which interacts with TBK1 activating IRF3 which binds as a dimer to the ISRE site of the IFNb and IP-10 genes PMID: 16930560,14530355 TRIF can also interact with TBK1/IKKe which leads to the activation of IRF3

PMID: 16930560,14530355 TRIF can also interact with TBK1/IKKe which leads to the activation of IRF3

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PMID: 16930560,14517278 TLR3 recruits TRIF to its TIR domain which interacts with TBK1 activating IRF3 which binds as a dimer to the ISRE site of the IFNb and IP-10 genes PMID: 16930560,14530355 TRIF can also interact with TBK1/IKKe which leads to the activation of IRF3

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PMID: 16930560,14517278 TLR3 recruits TRIF to its TIR domain which interacts with TBK1 activating IRF3 which binds as a dimer to the ISRE site of the IFNb and IP-10 genes PMID: 16930560,14530355 TRIF can also interact with TBK1/IKKe which leads to the activation of IRF3

PMID: 16930560,14517278 TLR3 recruits TRIF to its TIR domain which interacts with TBK1 activating IRF3 which binds as a dimer to the ISRE site of the IFNb and IP-10 genes

indirect

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PMID: 16930560,14517278 TLR3 recruits TRIF to its TIR domain which interacts with TBK1 activating IRF3 which binds as a dimer to the ISRE site of the IFNb and IP-10 genes PMID:16930560,12471095 IFN inducible genes are induced via the activation of IRF3 and other interferon inducible factors. LPS induction of IFN-inducible genes encoding IP-10, GARG-16 and IRG-1 was comparable in wild type,Mal-deficient andMyD88-deficientmacrophages

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PMID: 16930560,14517278 TLR3 recruits TRIF to its TIR domain which interacts with TBK1 activating IRF3 which binds as a dimer to the ISRE site of the IFNb and IP-10 genes

PMID: 16930560 TLR4 recruits TRAM to its TIR domain which in turn recruits TRIF and activates TBK1

PMID: 16930560 TLR4 recruits TRAM to its TIR domain which in turn recruits TRIF and activates TBK1

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PMID: 16930560 TLR4 recruits TRAM to its TIR domain which in turn recruits TRIF and activates TBK1

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PMID: 16930560 TBK1 activates IRF3

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PMID: 16930560 Under LPS stimulation p65 homodimers appear to interactwith IRF3 to activate the IP-10 gene PMID: 16930560,16143103 This IRF3/p65 complex is susceptible to glucocorticoid inhibition

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PMID: 16930560 Under LPS stimulation p65 homodimers appear to interactwith IRF3 to activate the IP-10 gene

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PMID:16930560,12471095 IFN inducible genes are induced via the activation of IRF3 and other interferon inducible factors. LPS induction of IFN-inducible genes encoding IP-10, GARG-16 and IRG-1 was comparable in wild type,Mal-deficient andMyD88-deficientmacrophages

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PMID:16930560,12471095 IFN inducible genes are induced via the activation of IRF3 and other interferon inducible factors. LPS induction of IFN-inducible genes encoding IP-10, GARG-16 and IRG-1 was comparable in wild type,Mal-deficient andMyD88-deficientmacrophages

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PMID:16930560,10565609 Orlicek et al., directly implicated Src kinases in LPS signalling to TNFa and iNOS (inducible nitric oxide synthase) induction with the use of the Src-selective inhibitor PP1, in murine macrophages

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PMID:16930560,10565609 Orlicek et al., directly implicated Src kinases in LPS signalling to TNFa and iNOS (inducible nitric oxide synthase) induction with the use of the Src-selective inhibitor PP1, in murine macrophages

PMID:16930560,16166516,16166517 TNFa expression is induced in an NFkB-independent IRF3-dependent manner, binds to the TNF receptor and induces NFkB activation providing delayed NFkB induction

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PMID:16930560,16166516,16166517 TNFa expression is induced in an NFkB-independent IRF3-dependent manner, binds to the TNF receptor and induces NFkB activation providing delayed NFkB induction

PMID: 16930560,11518704,12242293 Phosphorylation of TAK1 and TAB2 occurs initiating the dissociation of TRAF6/TAK1/TAB1/TAB2 from the membrane to the cytosol, and IRAK-1 degradation PMID: 16930560,11460167,11518704,12242293 Ubiquitination of TRAF6 and TAK1 activate the complex, and phosphorylation of TAK1 and TAB2 initiates the release of the complex from the membrane

PMID: 16930560,8011280 Once activated by a PAMP, a TLR triggers a cascade of cellular signals, culminating in the eventual activationofNFkBwhichbinds to a discretenucleotide sequence in the upstream regions of genes that produce proinflammatory cytokines, such as TNFa, IL-1, and IL-2, thereby regulating their expression

PMID: 16930560,8011280 Once activated by a PAMP, a TLR triggers a cascade of cellular signals, culminating in the eventual activationofNFkBwhichbinds to a discretenucleotide sequence in the upstream regions of genes that produce proinflammatory cytokines, such as TNFa, IL-1, and IL-2, thereby regulating their expression

PMID: 16930560,8011280 Once activated by a PAMP, a TLR triggers a cascade of cellular signals, culminating in the eventual activationofNFkBwhichbinds to a discretenucleotide sequence in the upstream regions of genes that produce proinflammatory cytokines, such as TNFa, IL-1, and IL-2, thereby regulating their expression

PMID: 16930560,14517278 TLR3 recruits TRIF to its TIR domain which interacts with TBK1 activating IRF3 which binds as a dimer to the ISRE site of the IFNb and IP-10 genes

PMID: 16930560,14517278 TLR3 recruits TRIF to its TIR domain which interacts with TBK1 activating IRF3 which binds as a dimer to the ISRE site of the IFNb and IP-10 genes