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PMID: 17621314, 17048703, 11432202, 16807108 Although nearly all TLRs recruit MyD88, only some recruit Mal, TRAM and TRIF, giving rise to specificity in signalling. PMID: 17621314, 7848516 sTLRs compete with TLR agonists and are highly effective in the first line of negative regulation, as they directly attenuate TLR signalling and therefore prevent acute inflammatory responses.

PMID: 17621314, 17048703, 11432202, 16807108 Although nearly all TLRs recruit MyD88, only some recruit Mal, TRAM and TRIF, giving rise to specificity in signalling.

PMID: 17621314, 15557191 The mechanism involved in sTLR-4 inhibition to date is not fully understood, however, it has been hypothesized that sTLR-4 may block the interaction between TLR-4 and its co-receptors MD2 and CD14, leading to the termination of signalling.

PMID: 17621314, 15557191 The mechanism involved in sTLR-4 inhibition to date is not fully understood, however, it has been hypothesized that sTLR-4 may block the interaction between TLR-4 and its co-receptors MD2 and CD14, leading to the termination of signalling. PMID: 17621314, 15557191 The mechanism involved in sTLR-4 inhibition to date is not fully understood, however, it has been hypothesized that sTLR-4 may block the interaction between TLR-4 and its co-receptors MD2 and CD14, leading to the termination of signalling.

PMID: 17621314, 12447442, 12447441 Mal plays a critical role in host response as demonstrated by the total absence of pro-inflammatory cytokine production during either TLR-2 or TLR-4 signalling.

PMID: 17621314 TRIF has been shown to be critical for signalling by lipopolysaccharide (LPS) via TLR-4 and for signalling by polyI:C via TLR-3, while TRAM was shown to be required for TLR-4 signalling only.

PMID: 17621314, 17048703, 16807108, 16698941 TRIF has been found to induce the expression of IFN-beta in response to TLR-4 and TLR-3 ligands. PMID: 17621314 To date, it is still unclear in regards to the exact mechanism of how SARM inhibits TRIF function, however, it can be hypothesized from finding by Bowie and colleagues, who demonstrated that SARM and TRIF weakly interact in resting cells and upon LPS stimulation, increase in stability possibly preventing the recruitment of downstream effector molecules to TRIF.

PMID: 17621314 TRIF has been shown to be critical for signalling by lipopolysaccharide (LPS) via TLR-4 and for signalling by polyI:C via TLR-3, while TRAM was shown to be required for TLR-4 signalling only.

PMID: 17621314, 17048703, 16807108, 16698941 TRIF has been found to induce the expression of IFN-beta in response to TLR-4 and TLR-3 ligands. PMID: 17621314 To date, it is still unclear in regards to the exact mechanism of how SARM inhibits TRIF function, however, it can be hypothesized from finding by Bowie and colleagues, who demonstrated that SARM and TRIF weakly interact in resting cells and upon LPS stimulation, increase in stability possibly preventing the recruitment of downstream effector molecules to TRIF.

PMID: 17621314, 16230348 Upon stimulation with PGN, MALP-2 and Pam3CSK-4 (ligands of TLR-2), cells displayed an enhanced activation and expression of NF-kappaB, TNF-alpha, IL-1beta and IL-8.

PMID: 17621314, 12447442, 12447441 Mal plays a critical role in host response as demonstrated by the total absence of pro-inflammatory cytokine production during either TLR-2 or TLR-4 signalling.

PMID: 17621314, 7848516 sTLRs compete with TLR agonists and are highly effective in the first line of negative regulation, as they directly attenuate TLR signalling and therefore prevent acute inflammatory responses.

PMID: 17621314, 11986301 sTLR-2 was found to inhibit IL-8 and tumour necrosis factor (TNF) through the direct interaction with co-receptor sCD14 following stimulation with bacterial lipopeptide.

PMID: 17621314, 11986301 sTLR-2 was found to inhibit IL-8 and tumour necrosis factor (TNF) through the direct interaction with co-receptor sCD14 following stimulation with bacterial lipopeptide.

PMID: 17621314, 12538665 Subsequent studies showed the preferential recruitment of MyD88s-MyD88 heterodimers in favour of MyD88 homodimers, which allowed the recruitment of IRAK-1 resulting in the ablation of IRAK-1 phosphorylation.

PMID: 17621314, 12538665 Subsequent studies showed the preferential recruitment of MyD88s-MyD88 heterodimers in favour of MyD88 homodimers, which allowed the recruitment of IRAK-1 resulting in the ablation of IRAK-1 phosphorylation. PMID: 17621314, 12885415 This phosphorylation is normally mediated by IRAK-4, but in the presence of MyD88s, IRAK-4 is not recruited to the signalling complex.

PMID: 17621314, 12538665 Subsequent studies showed the preferential recruitment of MyD88s-MyD88 heterodimers in favour of MyD88 homodimers, which allowed the recruitment of IRAK-1 resulting in the ablation of IRAK-1 phosphorylation.

PMID: 17621314, 12885415 This phosphorylation is normally mediated by IRAK-4, but in the presence of MyD88s, IRAK-4 is not recruited to the signalling complex. PMID: 17621314, 11751856 Tollip also interacts with IRAK-1 leading to a decrease in IRAK-1 autophosphorylation and NF-kappaB activation.

PMID: 17621314, 12150927 It was also discovered in vitro that IRAK-M prevents dissociation of IRAK-1/IRAK-4 from the MyD88 receptor complex, therefore inhibiting the association of IRAK-1 with TRAF-6.

PMID: 17621314, 12150927 It was also discovered in vitro that IRAK-M prevents dissociation of IRAK-1/IRAK-4 from the MyD88 receptor complex, therefore inhibiting the association of IRAK-1 with TRAF-6. PMID: 17621314 The exact mechanism of how TRAF-6 is targeted for the negative regulation of TLR-mediated signalling by FLN29 is undefined, however, it is suggested that FLN29 may inhibit downstream of TRAF-6 based on current findings.

PMID: 17621314, 15004556 This study showed a direct interaction between ST2L and MyD88 and Mal, but not TRIF or IRAK.

PMID: 17621314, 15004556 This study showed a direct interaction between ST2L and MyD88 and Mal, but not TRIF or IRAK.

PMID: 17621314, 11359817 sST2 binds to macrophages through a putative ST2 receptor.

Indirect

Indirect

PMID: 17621314, 15557191, 11359817 Following the addition of sST2 to LPS-stimulated macrophages, there was significant suppression of mRNA expression of TLR-1 and TLR-4, leading to reduced pro-inflammatory cytokine production.

Indirect

Indirect

PMID: 17621314, 15557191, 11359817 Following the addition of sST2 to LPS-stimulated macrophages, there was significant suppression of mRNA expression of TLR-1 and TLR-4, leading to reduced pro-inflammatory cytokine production. PMID: 17621314, 15623538 TGF-beta1 inhibits TLR-4 expression by suppressing LPS-mediated responses and is also able to induce MyD88 degradation through interactions via its DD.

Indirect

PMID: 17621314, 14993616 LPS stimulation in mouse models caused an increase in SIGIRR expression in various tissues, implicating its importance in the regulation of inflammatory responses.

PMID: 17621314, 12925853 Similarly to ST2, this suggests that SIGIRR acts on the MyD88-dependent pathway as SIGIRR has been shown to form complexes with IL-1 receptor complex molecules, IRAK and TRAF-6 upon IL-1 stimulation in vitro.

PMID: 17621314, 12925853 Similarly to ST2, this suggests that SIGIRR acts on the MyD88-dependent pathway as SIGIRR has been shown to form complexes with IL-1 receptor complex molecules, IRAK and TRAF-6 upon IL-1 stimulation in vitro.

PMID: 17621314, 12925853 Similarly to ST2, this suggests that SIGIRR acts on the MyD88-dependent pathway as SIGIRR has been shown to form complexes with IL-1 receptor complex molecules, IRAK and TRAF-6 upon IL-1 stimulation in vitro. PMID: 17621314, 10854325 Toll-interacting protein (Tollip) is a protein which interacts with the IL-1R accessory protein and is responsible for bringing IRAK to the receptor complex.

PMID: 17621314, 12925853 Similarly to ST2, this suggests that SIGIRR acts on the MyD88-dependent pathway as SIGIRR has been shown to form complexes with IL-1 receptor complex molecules, IRAK and TRAF-6 upon IL-1 stimulation in vitro. PMID: 17621314 The exact mechanism of how TRAF-6 is targeted for the negative regulation of TLR-mediated signalling by FLN29 is undefined, however, it is suggested that FLN29 may inhibit downstream of TRAF-6 based on current findings.

PMID: 17621314, 12925853 Similarly to ST2, this suggests that SIGIRR acts on the MyD88-dependent pathway as SIGIRR has been shown to form complexes with IL-1 receptor complex molecules, IRAK and TRAF-6 upon IL-1 stimulation in vitro.

Indirect

PMID: 17621314, 14715412 It was also shown that the overexpression of SIGIRR in bone marrow-derived DCs leads to the inhibition of IL-1 and -18-mediated activation of NF-kappaB. PMID: 17621314, 15852007 This was also observed in vivo as NF-kappaB activation was downregulated. PMID: 17621314, 15125834, 15173580 For example, beta-arrestin-1 and beta-arrestin-2 have been shown to directly interact with IkappaB-alpha, preventing its phosphorylation and subsequent degradation, as well as blocking TNF-induced phosphorylation and degradation of IkappaB-alpha. PMID: 17621314, 15125834, 15173580 beta-arrestin-1 and beta-arrestin-2 have recently been identified as negative regulators of TLR-IL-1R-mediated signalling pathways augmenting NF-kappaB activation.

PMID: 17621314, 15589175 After initial activation of the TLR signalling pathways, TRAILR appears to stabilize IkappaB-alpha resulting in the decrease of nuclear translocation of NF-kappaB. PMID: 17621314, 15334086 A20, was originally associated with TNF mediated NF-kappaB activation, but has also been identified as a cysteine protease de-ubiquitylating protein able to prevent TLR signalling via TRAF-6. Ablation of TLR-mediated signalling is the result of the cleavage of a polyubiquitin chain in TRAF-6 that in turn inhibits NFkappaB translocation to the nucleus.

PMID: 17621314, 15334086 A20, was originally associated with TNF mediated NF-kappaB activation, but has also been identified as a cysteine protease de-ubiquitylating protein able to prevent TLR signalling via TRAF-6. Ablation of TLR-mediated signalling is the result of the cleavage of a polyubiquitin chain in TRAF-6 that in turn inhibits NFkappaB translocation to the nucleus.

PMID: 17621314, 16426569 This study showed that sST2 suppressed the production of IL-6, IL-1beta and TNF-alpha by binding to THP-1 cells, in turn reducing the binding affinity of NF-kappaB to the IL-6 promoter, leading to the degradation of IkappaB following LPS stimulation.

Indirect

PMID: 17621314, 16426569 This study showed that sST2 suppressed the production of IL-6, IL-1beta and TNF-alpha by binding to THP-1 cells, in turn reducing the binding affinity of NF-kappaB to the IL-6 promoter, leading to the degradation of IkappaB following LPS stimulation. PMID: 17621314, 11986301 sTLR-2 was found to inhibit IL-8 and tumour necrosis factor (TNF) through the direct interaction with co-receptor sCD14 following stimulation with bacterial lipopeptide. PMID: 17621314, 16230348 Upon stimulation with PGN, MALP-2 and Pam3CSK-4 (ligands of TLR-2), cells displayed an enhanced activation and expression of NF-kappaB, TNF-alpha, IL-1beta and IL-8.

Indirect

PMID: 17621314, 16426569 This study showed that sST2 suppressed the production of IL-6, IL-1beta and TNF-alpha by binding to THP-1 cells, in turn reducing the binding affinity of NF-kappaB to the IL-6 promoter, leading to the degradation of IkappaB following LPS stimulation. PMID: 17621314, 16230348 Upon stimulation with PGN, MALP-2 and Pam3CSK-4 (ligands of TLR-2), cells displayed an enhanced activation and expression of NF-kappaB, TNF-alpha, IL-1beta and IL-8.

PMID: 17621314, 16303092 In order for inhibitory effects to be exerted by RP105, it requires its own coreceptor MD1 before an interaction with the TLR-4/MD2 complex is possible.

Indirect

PMID: 17621314, 16303092 In order for inhibitory effects to be exerted by RP105, it requires its own coreceptor MD1 before an interaction with the TLR-4/MD2 complex is possible. PMID: 17621314, 16303092 Divanovic et al., found that upon stimulation with LPS, RP105 directly interacts with the TLR-4/MD2 complex sequestering sites available for LPS binding.

PMID: 17621314, 15589175 After initial activation of the TLR signalling pathways, TRAILR appears to stabilize IkappaB-alpha resulting in the decrease of nuclear translocation of NF-kappaB.

PMID: 17621314, 16426569 This study showed that sST2 suppressed the production of IL-6, IL-1beta and TNF-alpha by binding to THP-1 cells, in turn reducing the binding affinity of NF-kappaB to the IL-6 promoter, leading to the degradation of IkappaB following LPS stimulation.

PMID: 17621314, 16426569 This study showed that sST2 suppressed the production of IL-6, IL-1beta and TNF-alpha by binding to THP-1 cells, in turn reducing the binding affinity of NF-kappaB to the IL-6 promoter, leading to the degradation of IkappaB following LPS stimulation. PMID: 17621314, 16670302 PI3K class I enzymes were shown to affect NF-kappaB activation and IL-12 production, where as the class III PI3Ks were shown to be involved in both NF-kappaB activation as well as the production of IL-6, IL-12 and TNF-alpha. PMID: 17621314, 16670302 In recent studies by Kuo et al., they demonstrated that the class I and class III PI3K enzymes have distinct negative regulatory roles in TLR signalling in response to CpG DNA/ODN.

PMID: 17621314, 16426569 This study showed that sST2 suppressed the production of IL-6, IL-1beta and TNF-alpha by binding to THP-1 cells, in turn reducing the binding affinity of NF-kappaB to the IL-6 promoter, leading to the degradation of IkappaB following LPS stimulation. PMID: 17621314, 16670302 PI3K class I enzymes were shown to affect NF-kappaB activation and IL-12 production, where as the class III PI3Ks were shown to be involved in both NF-kappaB activation as well as the production of IL-6, IL-12 and TNF-alpha. PMID: 17621314, 16670302 In recent studies by Kuo et al., they demonstrated that the class I and class III PI3K enzymes have distinct negative regulatory roles in TLR signalling in response to CpG DNA/ODN. PMID: 17621314, 16221674 Mashima et al., found FLN29 overexpression in macrophage RAW cells stimulated with LPS caused a significant decrease in TNF-alpha and nitric oxide activation and production.

PMID: 17621314, 16426569 This study showed that sST2 suppressed the production of IL-6, IL-1beta and TNF-alpha by binding to THP-1 cells, in turn reducing the binding affinity of NF-kappaB to the IL-6 promoter, leading to the degradation of IkappaB following LPS stimulation.

Indirect

PMID: 17621314, 16286016 It must be noted that there are conflicting reports on the actions of ST2, as Schmitz et al. recently described that ST2 was a receptor for the recently identified member of the IL-1 family namely IL-33, which exerts its biological effects via ST2 enhancing activation of NF-kappaB and MAPK. PMID: 17621314, 15125834, 15173580 For example, beta-arrestin-1 and beta-arrestin-2 have been shown to directly interact with IkappaB-alpha, preventing its phosphorylation and subsequent degradation, as well as blocking TNF-induced phosphorylation and degradation of IkappaB-alpha.

PMID: 17621314, 11120784 It was demonstrated in mouse models that the presence of sTLR-4 following LPS stimulation inhibited NF-kappaB activation in vitro.

Indirect

Indirect

PMID: 17621314 The treatment of cells with LPS resulted in significantly increased levels of SARM proteins, suggesting a mechanism for how SARM is involved in specifically regulating TRIF-dependent TLR-3 and TLR-4 inflammatory esponses through a negative-feedback mechanism.

Indirect

PMID: 17621314 To date, it is still unclear in regards to the exact mechanism of how SARM inhibits TRIF function, however, it can be hypothesized from finding by Bowie and colleagues, who demonstrated that SARM and TRIF weakly interact in resting cells and upon LPS stimulation, increase in stability possibly preventing the recruitment of downstream effector molecules to TRIF.

Indirect

Indirect

PMID: 17621314, 15082713 IRAK-2a and IRAK-2b were found in overexpression studies to enhance NFkappaB activation. PMID: 17621314, 15082713 The overexpression of IRAK-2c and IRAK-2d, which lack the N-terminal DD, were shown in fibroblasts to have inhibitory effects on NF-kappaB activation following LPS stimulation. PMID: 17621314, 15125834, 15173580 For example, beta-arrestin-1 and beta-arrestin-2 have been shown to directly interact with IkappaB-alpha, preventing its phosphorylation and subsequent degradation, as well as blocking TNF-induced phosphorylation and degradation of IkappaB-alpha.

Indirect

Indirect

PMID: 17621314, 15082713 IRAK-2a and IRAK-2b were found in overexpression studies to enhance NFkappaB activation. PMID: 17621314, 15082713 The overexpression of IRAK-2c and IRAK-2d, which lack the N-terminal DD, were shown in fibroblasts to have inhibitory effects on NF-kappaB activation following LPS stimulation. PMID: 17621314, 15125834, 15173580 For example, beta-arrestin-1 and beta-arrestin-2 have been shown to directly interact with IkappaB-alpha, preventing its phosphorylation and subsequent degradation, as well as blocking TNF-induced phosphorylation and degradation of IkappaB-alpha.

PMID: 17621314, 10854325 Toll-interacting protein (Tollip) is a protein which interacts with the IL-1R accessory protein and is responsible for bringing IRAK to the receptor complex.

PMID: 17621314, 11751856 There are three known isoforms of Tollip, however, Tollip-1 has been shown to bind TLR-2 and TLR-4, and in overexpression studies leads to the subsequent inhibition of NF-kappaB activation.

PMID: 17621314, 11751856 There are three known isoforms of Tollip, however, Tollip-1 has been shown to bind TLR-2 and TLR-4, and in overexpression studies leads to the subsequent inhibition of NF-kappaB activation.

PMID: 17621314, 11751856 Tollip also interacts with IRAK-1 leading to a decrease in IRAK-1 autophosphorylation and NF-kappaB activation.

Indirect

PMID: 17621314, 11751856 Tollip also interacts with IRAK-1 leading to a decrease in IRAK-1 autophosphorylation and NF-kappaB activation. PMID: 17621314, 11751856 There are three known isoforms of Tollip, however, Tollip-1 has been shown to bind TLR-2 and TLR-4, and in overexpression studies leads to the subsequent inhibition of NF-kappaB activation. PMID: 17621314, 15334086 A20, was originally associated with TNF mediated NF-kappaB activation, but has also been identified as a cysteine protease de-ubiquitylating protein able to prevent TLR signalling via TRAF-6. Ablation of TLR-mediated signalling is the result of the cleavage of a polyubiquitin chain in TRAF-6 that in turn inhibits NFkappaB translocation to the nucleus. PMID: 17621314 Investigators identified that SOCS-1 directly inhibits Mal-dependent p65 phosphorylation and subsequent NF-kappaB transactivation. PMID: 17621314, 15125834, 15173580 For example, beta-arrestin-1 and beta-arrestin-2 have been shown to directly interact with IkappaB-alpha, preventing its phosphorylation and subsequent degradation, as well as blocking TNF-induced phosphorylation and degradation of IkappaB-alpha. PMID: 17621314, 15125834, 15173580 beta-arrestin-1 and beta-arrestin-2 have recently been identified as negative regulators of TLR-IL-1R-mediated signalling pathways augmenting NF-kappaB activation. PMID: 17621314, 16378096 The binding of beta-arrestins to the TRAF-N domain in TRAF-6 prevents autoubiquitination, thus preventing downstream activation of NF-kappaB and AP- 1 Wang et al. PMID: 17621314, 16670302 PI3K class I enzymes were shown to affect NF-kappaB activation and IL-12 production, where as the class III PI3Ks were shown to be involved in both NF-kappaB activation as well as the production of IL-6, IL-12 and TNF-alpha. PMID: 17621314, 16670302 In recent studies by Kuo et al., they demonstrated that the class I and class III PI3K enzymes have distinct negative regulatory roles in TLR signalling in response to CpG DNA/ODN. PMID: 17621314, 10385526, 11390377 LIND has been identified as an LPS-inducible A20-binding inhibitor of NFkappa-B and shares sequence homology to A20-binding inhibitor of NF-kappaB activation (ABIN)–1 and ABIN-2. PMID: 17621314, 17088249 Subsequent coexpression studies using MyD88, IRAK-1, TRAF-6 and downstream IKKbeta with ABIN-3 revealed that ABIN-3 inhibits MyD88, IRAK-1 and TRAF-6-mediated NF-kappaB activation, however has no effect on IKKbeta induced activation. PMID: 17621314 Further investigations by Wang et al. revealed that Fliih was able to inhibit TLR-4–MyD88-dependent activation of NF-kappaB. PMID: 17621314 Furthermore, overexpression studies in HEK-293 cells cotransfected with TLR-2, TLR-3, TLR-4 and TLR-9, stimulated with their appropriate ligands and increasing doses of TRAF-4, resulted in luciferase analysis showing a decrease in activation of both NF-kappaB and the IFN-beta promoter, but not in TNF-alpha receptor-mediated signalling.

PMID: 17621314 With decreasing levels of IRAK-1 phosphorylation, it has been observed there is an increase in Tollip phosphorylation.

PMID: 17621314, 11751856 This is though to be a mechanism that allows the release of Tollip from the Tollip/IRAK-1 complex resulting in the termination of its negative regulatory actions.

Indirect

PMID: 17621314, 1381359, 2118515 A20 is a zinc ring finger protein which is expressed in numerous cell types and rapidly increases in expression in response to LPS and TNF, implicating it as a possible regulator of inflammatory responses.

Indirect

PMID: 17621314, 1381359, 2118515 A20 is a zinc ring finger protein which is expressed in numerous cell types and rapidly increases in expression in response to LPS and TNF, implicating it as a possible regulator of inflammatory responses.

Indirect

PMID: 17621314, 15334086 A20, was originally associated with TNF mediated NF-kappaB activation, but has also been identified as a cysteine protease de-ubiquitylating protein able to prevent TLR signalling via TRAF-6. Ablation of TLR-mediated signalling is the result of the cleavage of a polyubiquitin chain in TRAF-6 that in turn inhibits NFkappaB translocation to the nucleus. PMID: 17621314, 16378096 The binding of beta-arrestins to the TRAF-N domain in TRAF-6 prevents autoubiquitination, thus preventing downstream activation of NF-kappaB and AP- 1 Wang et al. PMID: 17621314, 11057907 Ubc13 E2 ubiquitin-conjugating enzyme is known to olyubiquitinate TRAF-2 and TRAF-6 through their attached K63 polyubiquitin chains.

PMID: 17621314, 15107846 Triad3A when overexpressed results in substantial degradation of TLR-4 and TLR-9, which lead to a decrease in signal transduction, but did not effect TLR-2 or TLR-3 mediated signalling.

Indirect

PMID: 17621314, 15107846 Triad3A when overexpressed results in substantial degradation of TLR-4 and TLR-9, which lead to a decrease in signal transduction, but did not effect TLR-2 or TLR-3 mediated signalling.

Indirect

PMID: 17621314, 16968706 Recent studies have also suggested that Triad3A is able to target other TIR domain-containing adaptors including RIP-1, TRIF and Mal.

Indirect

PMID: 17621314, 16968706 Recent studies have also suggested that Triad3A is able to target other TIR domain-containing adaptors including RIP-1, TRIF and Mal.

PMID: 17621314, 16968706 Recent studies have also suggested that Triad3A is able to target other TIR domain-containing adaptors including RIP-1, TRIF and Mal.

Indirect

PMID: 17621314, 12433365, 12433373 LPS induces SOC-1 expression in macrophages and SOCS-1-/- mice are hypersensitive to LPS-induced endotoxic shock.

PMID: 17621314, 16415872 Recent investigations by Mansell et al. have shown the mechanism for SOCS-1 directly regulating TLR-2 and TLR-4-mediated signalling by argeting Mal for polyubiquitination and subsequent proteosomal degradation.

PMID: 17621314, 16415872 Recent investigations by Mansell et al. have shown the mechanism for SOCS-1 directly regulating TLR-2 and TLR-4-mediated signalling by argeting Mal for polyubiquitination and subsequent proteosomal degradation.

Indirect

PMID: 17621314, 16415872 Activation of Brunton’s tyrosine kinase is critical for mediating the Mal and SOCS-1 interaction (acting as an E3 ubiquitin ligase) resulting in Mal polyubiquitination and subsequent proteosomal degradation.

PMID: 17621314 The coupling of beta-arrestins to the GPCRs occurs following binding of a ligand to the appropriate receptor.

PMID: 17621314, 10995467, 10725339, 11861753 Beta-arrestins are adaptor molecules that are able to form complexes with G protein–coupled receptors (GPCRs), are involved in the desensitization and endocytosis of various cell surface receptors as well as being shown to bind molecules involved in the MAP signalling pathway including Erk-1/-2, JNK, p38 and members of the Src kinase family.

PMID: 17621314, 10995467, 10725339, 11861753 Beta-arrestins are adaptor molecules that are able to form complexes with G protein–coupled receptors (GPCRs), are involved in the desensitization and endocytosis of various cell surface receptors as well as being shown to bind molecules involved in the MAP signalling pathway including Erk-1/-2, JNK, p38 and members of the Src kinase family. PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314, 10995467, 10725339, 11861753 Beta-arrestins are adaptor molecules that are able to form complexes with G protein–coupled receptors (GPCRs), are involved in the desensitization and endocytosis of various cell surface receptors as well as being shown to bind molecules involved in the MAP signalling pathway including Erk-1/-2, JNK, p38 and members of the Src kinase family. PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314, 10995467, 10725339, 11861753 Beta-arrestins are adaptor molecules that are able to form complexes with G protein–coupled receptors (GPCRs), are involved in the desensitization and endocytosis of various cell surface receptors as well as being shown to bind molecules involved in the MAP signalling pathway including Erk-1/-2, JNK, p38 and members of the Src kinase family. PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314, 10995467, 10725339, 11861753 Beta-arrestins are adaptor molecules that are able to form complexes with G protein–coupled receptors (GPCRs), are involved in the desensitization and endocytosis of various cell surface receptors as well as being shown to bind molecules involved in the MAP signalling pathway including Erk-1/-2, JNK, p38 and members of the Src kinase family. PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314 This results in the interaction of b-arrestins with the signalling complexes and the subsequent mediation of phosphorylation and ubiquitination of MAP kinase target molecules.

PMID: 17621314, 15125834, 15173580 For example, beta-arrestin-1 and beta-arrestin-2 have been shown to directly interact with IkappaB-alpha, preventing its phosphorylation and subsequent degradation, as well as blocking TNF-induced phosphorylation and degradation of IkappaB-alpha.

PMID: 17621314, 15125834, 15173580 For example, beta-arrestin-1 and beta-arrestin-2 have been shown to directly interact with IkappaB-alpha, preventing its phosphorylation and subsequent degradation, as well as blocking TNF-induced phosphorylation and degradation of IkappaB-alpha.

Indirect

PMID: 17621314, 15125834, 15173580 For example, beta-arrestin-1 and beta-arrestin-2 have been shown to directly interact with IkappaB-alpha, preventing its phosphorylation and subsequent degradation, as well as blocking TNF-induced phosphorylation and degradation of IkappaB-alpha.

PMID: 17621314, 16378096 Wang et al., demonstrated using overexpression studies in HEK-293 cells, that beta-arrestin-1 and beta-arrestin-2 co-immunoprecipitated with TRAF-6, showing direct interactions.

PMID: 17621314, 16378096 Wang et al., demonstrated using overexpression studies in HEK-293 cells, that beta-arrestin-1 and beta-arrestin-2 co-immunoprecipitated with TRAF-6, showing direct interactions.

Indirect

PMID: 17621314, 16378096 The binding of beta-arrestins to the TRAF-N domain in TRAF-6 prevents autoubiquitination, thus preventing downstream activation of NF-kappaB and AP- 1 Wang et al.

Indirect

Indirect

PMID: 17621314, 17418896 Further studies also revealed that both bera-arrestin-1 and beta-arrestin-2 depletion using siRNA transfection resulted in the marked decrease of IL-8 production following LPS treatment.

Indirect

PMID: 17621314, 16670302 PI3K class I enzymes were shown to affect NF-kappaB activation and IL-12 production, where as the class III PI3Ks were shown to be involved in both NF-kappaB activation as well as the production of IL-6, IL-12 and TNF-alpha. PMID: 17621314, 16670302 PI3K class I enzymes were shown to affect NF-kappaB activation and IL-12 production, where as the class III PI3Ks were shown to be involved in both NF-kappaB activation as well as the production of IL-6, IL-12 and TNF-alpha. PMID: 17621314, 16670302 In recent studies by Kuo et al., they demonstrated that the class I and class III PI3K enzymes have distinct negative regulatory roles in TLR signalling in response to CpG DNA/ODN.

PMID: 17621314, 15623538 TGF-beta1 inhibits TLR-4 expression by suppressing LPS-mediated responses and is also able to induce MyD88 degradation through interactions via its DD.

PMID: 17621314, 15623538 TGF-beta1 inhibits TLR-4 expression by suppressing LPS-mediated responses and is also able to induce MyD88 degradation through interactions via its DD.

Indirect

Indirect

PMID: 17621314, 15330257 IL-10 is also shown to inhibit the production of pro-inflammatory cytokines through LPS, and in human DCs is known to downregulate IL-12 production through TLR-3- and TLR-4-mediated signalling.

Indirect

Indirect

PMID: 17621314, 15330257 IL-10 is also shown to inhibit the production of pro-inflammatory cytokines through LPS, and in human DCs is known to downregulate IL-12 production through TLR-3- and TLR-4-mediated signalling.

PMID: 17621314, 12161427 Previous studies have shown that ATF-3 is able to protect endothelial cells against TNF-induced apoptosis by decreasing p53 transcription.

Indirect

PMID: 17621314, 12161427 Previous studies have shown that ATF-3 is able to protect endothelial cells against TNF-induced apoptosis by decreasing p53 transcription.

PMID: 17621314, 10385526, 11390377 LIND has been identified as an LPS-inducible A20-binding inhibitor of NFkappa-B and shares sequence homology to A20-binding inhibitor of NF-kappaB activation (ABIN)–1 and ABIN-2.

Indirect

PMID: 17621314, 10385526, 11390377 LIND has been identified as an LPS-inducible A20-binding inhibitor of NFkappa-B and shares sequence homology to A20-binding inhibitor of NF-kappaB activation (ABIN)–1 and ABIN-2.

Indirect

PMID: 17621314, 16424162 Flightless I homolog (Fliih), primarily expressed in the cytoplasm, was identified as a MyD88 interacting partner in murine macrophages stimulated with lipid A.

PMID: 17621314, 16424162 Co-immunoprecipitation studies using HEK-293T cells expressing TLR-4 showed that Fliih directly interferes with the interaction of MyD88 and TLR-4 upon LPS stimulation.

PMID: 17621314 Further investigations using RAW cells overexpressing FLN29 showed an interaction with endogenous TRAF-6.

Indirect

PMID: 17621314, 16221674 Mashima et al., found FLN29 overexpression in macrophage RAW cells stimulated with LPS caused a significant decrease in TNF-alpha and nitric oxide activation and production.

PMID: 17621314, 16230348 Upon stimulation with PGN, MALP-2 and Pam3CSK-4 (ligands of TLR-2), cells displayed an enhanced activation and expression of NF-kappaB, TNF-alpha, IL-1beta and IL-8.

PMID: 17621314, 16230348 Upon stimulation with PGN, MALP-2 and Pam3CSK-4 (ligands of TLR-2), cells displayed an enhanced activation and expression of NF-kappaB, TNF-alpha, IL-1beta and IL-8.

Indirect

PMID: 17621314, 16230348 Upon stimulation with PGN, MALP-2 and Pam3CSK-4 (ligands of TLR-2), cells displayed an enhanced activation and expression of NF-kappaB, TNF-alpha, IL-1beta and IL-8. PMID: 17621314, 16230348 Yoshida et al. identified that CYLD is induced through recognition of TLR-2 ligands during bacterial infection, and is able to inhibit activation of both NF-kB and MAPK p38, leading to the subsequent inhibition of pro-inflammatory cytokines through a negative-feedback mechanism. .

Indirect

PMID: 17621314, 16230348 Upon stimulation with PGN, MALP-2 and Pam3CSK-4 (ligands of TLR-2), cells displayed an enhanced activation and expression of NF-kappaB, TNF-alpha, IL-1beta and IL-8. PMID: 17621314, 11986301 sTLR-2 was found to inhibit IL-8 and tumour necrosis factor (TNF) through the direct interaction with co-receptor sCD14 following stimulation with bacterial lipopeptide.

Indirect

PMID: 17621314, 16230348 Yoshida et al. identified that CYLD is induced through recognition of TLR-2 ligands during bacterial infection, and is able to inhibit activation of both NF-kB and MAPK p38, leading to the subsequent inhibition of pro-inflammatory cytokines through a negative-feedback mechanism. .

Indirect

PMID: 17621314, 16230348 Yoshida et al. identified that CYLD is induced through recognition of TLR-2 ligands during bacterial infection, and is able to inhibit activation of both NF-kB and MAPK p38, leading to the subsequent inhibition of pro-inflammatory cytokines through a negative-feedback mechanism. .

PMID: 17621314 Further co-immunoprecipitation studies demonstrated interactions of CYLD with TRAF-6 and TRAF-7, and colocalization studies confirmed this finding.

PMID: 17621314 Further co-immunoprecipitation studies demonstrated interactions of CYLD with TRAF-6 and TRAF-7, and colocalization studies confirmed this finding.

PMID: 17621314, 10627275, 12184814 Eleven mammalian DUSPs have been identified to contain an MAPK binding domain and of those DUSP-1 and DUSP-2 (also known as phosphatase of activated cells-1 (PAC-1)) are most closely affiliated with immune cells.

PMID: 17621314, 16286016 It must be noted that there are conflicting reports on the actions of ST2, as Schmitz et al. recently described that ST2 was a receptor for the recently identified member of the IL-1 family namely IL-33, which exerts its biological effects via ST2 enhancing activation of NF-kappaB and MAPK.

Indirect

Indirect

PMID: 17621314, 12444149, 15590669, 15485842 DUSP-1 overexpression in vitro using macrophages was shown to inhibit phosphorylation of MAPK resulting in the decreased expression of pro-inflammatory cytokines TNF-alpha and IL-6 in response to various TLR ligands.

Indirect

PMID: 17621314, 12444149, 15590669, 15485842 DUSP-1 overexpression in vitro using macrophages was shown to inhibit phosphorylation of MAPK resulting in the decreased expression of pro-inflammatory cytokines TNF-alpha and IL-6 in response to various TLR ligands.

Indirect

PMID: 17621314, 12444149, 15590669, 15485842 DUSP-1 overexpression in vitro using macrophages was shown to inhibit phosphorylation of MAPK resulting in the decreased expression of pro-inflammatory cytokines TNF-alpha and IL-6 in response to various TLR ligands.

PMID: 17621314 Furthermore, co-immunoprecipitation studies showed a physical interaction between DUSP-2 and p38, Jnk and Erk.

PMID: 17621314 Furthermore, co-immunoprecipitation studies showed a physical interaction between DUSP-2 and p38, Jnk and Erk.

PMID: 17621314 Furthermore, co-immunoprecipitation studies showed a physical interaction between DUSP-2 and p38, Jnk and Erk.

Indirect

PMID: 17621314 DUSP-2/PAC-1 is primarily known for its role in inactivating p38 and ERK in vitro.

Indirect

PMID: 17621314 Co-immunoprecipitation studies using the HEK-293-TLR-2 cells showed that CYLD acted as a negative regulator of the MAPK p38 pathway, as CYLD inhibited PGN-induced phosphorylation of IkappaB-alpha, MKK3/6 and p38.

PMID: 17621314, 17157040 It was shown through a series of mutational analyses that SHP-2 could bind specifically to the N terminus of TBK-1 to exert inhibitory effects on downstream signalling, as the binding of SHP-2 to TBK-1 suppresses TBK-1-mediated phosphorylation and subsequent cytokine production.

PMID: 17621314, 17157040 It was shown through a series of mutational analyses that SHP-2 could bind specifically to the N terminus of TBK-1 to exert inhibitory effects on downstream signalling, as the binding of SHP-2 to TBK-1 suppresses TBK-1-mediated phosphorylation and subsequent cytokine production.

Indirect

PMID: 17621314 IRF-3 activation was also shown to be inhibited in the presence of SHP-2 as RAW cells transfected with increasing doses of SHP-2 dose dependently decreased IRF-3 activation.

Indirect

PMID: 17621314 IRF-3 activation was also shown to be inhibited in the presence of SHP-2 as RAW cells transfected with increasing doses of SHP-2 dose dependently decreased IRF-3 activation.

Indirect

Indirect

PMID: 17621314, 17157040 SH-2 containing protein tyrosine phosphatase-2 (SHP-2) has been implicated as a negative regulator of IFN-beta production through TLR-3 and TLR-4-mediated signalling. PMID: 17621314 This results in the inhibition of IRF-3 in response to TLR-3 and TLR-4.

PMID: 17621314, 16699525 Peptidyl-prolyl isomerase (Pin)-1, consisting of a short N-terminal domain and a catalytic C-terminal domain is only able to directly interact with IRF-3 after IRF-3 has been phosphorylated on Ser 339.

PMID: 17621314 The mechanism involved in negatively regulating IRF-3 is achieved by Pin-1 binding directly to IRF-3 leading to its polyubiquitination and subsequent proteosomal degradation.

PMID: 17621314 The mechanism involved in negatively regulating IRF-3 is achieved by Pin-1 binding directly to IRF-3 leading to its polyubiquitination and subsequent proteosomal degradation.

PMID: 17621314, 14690596 Through mutational analyses of critical binding sites on the p65 subunit, the Thr254-Pro binding site was identified as critical for Pin-1 interactions.

PMID: 17621314 Without interactions at Thr-254, p65 cannot be phosphorylated, resulting in the p65 protein being unstable for the subsequent translocation into the nucleus and its targeting for proteosomal degradation.

PMID: 17621314 Without interactions at Thr-254, p65 cannot be phosphorylated, resulting in the p65 protein being unstable for the subsequent translocation into the nucleus and its targeting for proteosomal degradation.

PMID: 17621314 Without interactions at Thr-254, p65 cannot be phosphorylated, resulting in the p65 protein being unstable for the subsequent translocation into the nucleus and its targeting for proteosomal degradation.

PMID: 17621314 Further studies looking at the negative regulatory effects of SOCS-1 on p65 showed that SOCS-1 binds in an area of close proximity to that of Pin-1.

PMID: 17621314 As SOCS-1 is known to polyubiquitination p65 and suppress NF-kappaB activation, Ryo et al. wanted to investigate if SOCS-1 had any effect on the stability and ubiquitination of p65 in the presence of Pin-1. PMID: 17621314 Overexpression studies both in vitro and in vivo of SOCS-1, SOCS-1 mutant and Pin-1 showed that Pin-1 protects p65 from SOCS-1 destabilization through blocking its degradation, and was also able to inhibit SOCS-1-mediated ubiquitination.

PMID: 17621314 Overexpression studies both in vitro and in vivo of SOCS-1, SOCS-1 mutant and Pin-1 showed that Pin-1 protects p65 from SOCS-1 destabilization through blocking its degradation, and was also able to inhibit SOCS-1-mediated ubiquitination.

Indirect

PMID: 17621314, 11057907 Ubc13 E2 ubiquitin-conjugating enzyme is known to olyubiquitinate TRAF-2 and TRAF-6 through their attached K63 polyubiquitin chains.

Indirect

PMID: 17621314 TRAF-6 and TRAF-2 are involved in the ubiquitination of downstream adaptor molecule NF-kappaB essential modulator (NEMO) in response to antigen receptor induced NF-kappaB activation.

Indirect

PMID: 17621314 TRAF-6 and TRAF-2 are involved in the ubiquitination of downstream adaptor molecule NF-kappaB essential modulator (NEMO) in response to antigen receptor induced NF-kappaB activation.

Indirect

Indirect

PMID: 17621314 DUSP-2/PAC-1 is primarily known for its role in inactivating p38 and ERK in vitro.

Indirect

PMID: 17621314 Results indicated that phosphorylation of Jnk and p38 was significantly reduced in Ubc13f l/f l Cd19 Cre B cells upon stimulation with anti-IgM compared to wild type.

Indirect

Indirect

PMID: 17621314 Phosphorylation of signalling adaptor NEMO in vitro has been suggested to be dependent on Ubc13 under IL-1beta induction.

PMID: 17621314, 12974773 Studies have revealed that mycobacteria directly interact with DC-SIGN in order to regulate TLR-4 mediated signalling responses in DCs. PMID: 17621314, 12974773 Specifically the ligand responsible for modulating TLR-4 responses is ManLAM, a cell-wall component of Mycobacterium tuberculosis. The mechanism by which ManLAM negatively regulates TLR-4 is by binding to DC-SIGN, impairing LPS-induced DC maturation and the marked increase of IL-10 that has known immunosuppressive properties.

PMID: 17621314, 12974773 Specifically the ligand responsible for modulating TLR-4 responses is ManLAM, a cell-wall component of Mycobacterium tuberculosis. The mechanism by which ManLAM negatively regulates TLR-4 is by binding to DC-SIGN, impairing LPS-induced DC maturation and the marked increase of IL-10 that has known immunosuppressive properties.

Indirect

Indirect

PMID: 17621314, 12974773 Specifically the ligand responsible for modulating TLR-4 responses is ManLAM, a cell-wall component of Mycobacterium tuberculosis. The mechanism by which ManLAM negatively regulates TLR-4 is by binding to DC-SIGN, impairing LPS-induced DC maturation and the marked increase of IL-10 that has known immunosuppressive properties.

Indirect

Indirect

PMID: 17621314, 17462920 ManLAM binds DC-SIGN in human DCs modulating TLR signalling by activating the serine and threonine kinase Raf-1, allowing the subsequent phosphorylation and acetylation of the p65 unit of NF-kappaB. PMID: 17621314, 17462920 Further investigations revealed that the specific phosphorylation event of Ser 276 on p65 is critical for Raf-1-dependent acetylation and the prolonged transcription of the IL-10 gene.

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PMID: 17621314, 17462920 Further investigations revealed that the specific phosphorylation event of Ser 276 on p65 is critical for Raf-1-dependent acetylation and the prolonged transcription of the IL-10 gene.

Indirect

PMID: 17621314 Two consequences of p65 acetylation are, first, the increased expression of IL-10 and, second, there is a prolonged activation of p65 and therefore prolonged NF-kappaB activity allowing increased transcription of the IL-10 gene.

PMID: 17621314, 16052631 Takeshita et al., using cytosolic components of nicotinamide adenine dinucleotide phosphate oxidase, namely p47phox, p67phox, p40phox and rac2, described the interaction between p47phox and TRAF-4 resulting in the suppression of TLR-mediated signalling through TRAF-6 and TRIF.

PMID: 17621314, 16052631 Following this observation, co-immunoprecipitation studies confirmed a physical interaction with not only p47phox, but also with TRAF-6, TRIF and IRAK-1, suggesting that TRAF-4 is able to form complexes with these molecules. PMID: 17621314, 16052631 Possible mechanisms suggested by Takeshita et al., for the negative regulation of TLR-mediated signalling by NADH oxidase is via a novel TRAF–TRAF dimerization, through the interaction of p47phox with TRAF-4, TRAF-6 and TRIF.

PMID: 17621314 Furthermore, overexpression studies in HEK-293 cells cotransfected with TLR-2, TLR-3, TLR-4 and TLR-9, stimulated with their appropriate ligands and increasing doses of TRAF-4, resulted in luciferase analysis showing a decrease in activation of both NF-kappaB and the IFN-beta promoter, but not in TNF-alpha receptor-mediated signalling.