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PMID: 18631453, 15795223
In brief, the model currently used to describe initiation of signaling involves ligand-induced dimerization of TLRs, creating a TIR-TIR interface, which acts to recruit adapters via their TIR domains.
PMID: 18631453
MyD88 is the universal adaptor, used by all TLRs except TLR3, and acts to recruit the IRAK family of kinases.
PMID: 18631453, 18327267
A uropathogenic strain of E. coli, termed CFT073, was then shown to have a TIR-domain-containing protein termed TIR-containing protein C (TcpC). The bacteria release this protein, which is somehow taken up by macrophages, where it interacts with MyD88 to prevent signaling.
PMID: 18631453
The best characterized are TLR2, which in combination with TLR1 or TLR6 can recognize acylated lipopeptides; TLR3, which senses double-stranded RNA; TLR4, which senses LPS; and TLR9, which senses hypomethylated CpG motifs.
PMID: 18631453
MyD88 adaptor-like (Mal, also called TIRAP) is recruited by TLR2 and TLR4, and so far its main function appears to be to subsequently stabilize MyD88 in the complex, acting as a bridge.
PMID: 18631453
The best characterized are TLR2, which in combination with TLR1 or TLR6 can recognize acylated lipopeptides; TLR3, which senses double-stranded RNA; TLR4, which senses LPS; and TLR9, which senses hypomethylated CpG motifs.
PMID: 18631453
The best characterized are TLR2, which in combination with TLR1 or TLR6 can recognize acylated lipopeptides; TLR3, which senses double-stranded RNA; TLR4, which senses LPS; and TLR9, which senses hypomethylated CpG motifs.
PMID: 18631453
MyD88 adaptor-like (Mal, also called TIRAP) is recruited by TLR2 and TLR4, and so far its main function appears to be to subsequently stabilize MyD88 in the complex, acting as a bridge.
PMID: 18631453
TLR3, which senses double-stranded RNA.
PMID: 18631453
The best characterized are TLR2, which in combination with TLR1 or TLR6 can recognize acylated lipopeptides; TLR3, which senses double-stranded RNA; TLR4, which senses LPS; and TLR9, which senses hypomethylated CpG motifs.
PMID: 18631453, 17572678
In the case of TLR9, it has been shown that a pre-exising dimer occurs, which presumably “tightens” upon ligand binding to create a new conformation.
PMID: 18631453, 17967410
NLRs that have been assigned functions include NOD1 and NOD2, which sense iE-DAP and MDP, respectively.
PMID: 18631453, 17967410
NLRs that have been assigned functions include NOD1 and NOD2, which sense iE-DAP and MDP, respectively.
PMID: 18631453, 15530394, 16407889, 18403674
In addition, Nalp3 (also called Cryopyrin of Nlrp3) senses multiple pathogens, pathogen products such as MDP, and products of damaged cells such as uric acid crystals and exogenous crystals such as asbestos.
PMID: 18631453, 15530394, 16407889, 18403674
In addition, Nalp3 (also called Cryopyrin of Nlrp3) senses multiple pathogens, pathogen products such as MDP, and products of damaged cells such as uric acid crystals and exogenous crystals such as asbestos.
PMID: 18631453, 15530394, 16407889, 18403674
In addition, Nalp3 (also called Cryopyrin of Nlrp3) senses multiple pathogens, pathogen products such as MDP, and products of damaged cells such as uric acid crystals and exogenous crystals such as asbestos.
PMID: 18631453, 15208624, 12163569
The best-known RLR is RIG-I, which senses single-stranded RNA found in viruses, and the best known CLR is Dectin-1, which senses beta-glucan, found in fungal cell walls.
PMID: 18631453, 15208624, 12163569
The best-known RLR is RIG-I, which senses single-stranded RNA found in viruses, and the best known CLR is Dectin-1, which senses beta-glucan, found in fungal cell walls.
PMID: 18631453, 15795223
In brief, the model currently used to describe initiation of signaling involves ligand-induced dimerization of TLRs, creating a TIR-TIR interface, which acts to recruit adapters via their TIR domains.
PMID: 18631453
This in turn leads to the recruitment of IRAK1 and IRAK4.
PMID: 18631453
IRAK4 and IRAK1 (and probably IRAK2) are then recruited to MyD88.
PMID: 18631453
IRAK4 then activates IRAK1, allowing IRAK1 to autophosphorylate.
PMID: 18631453
IRAK4 then activates IRAK1, allowing IRAK1 to autophosphorylate.
PMID; 18631453
Both IRAK1 and IRAK4 then dissociate from MyD88, which remains in a complex with the activated receptor—this has been shown for IL-1RI and will most probably apply to the TLRs.
PMID: 18631453
IRAK4 then phosphorylates IRAK1, and the kinases dissociate from MyD88.
PMID: 18631453
They in turn interact with TRAF6, which is an E3 ubiquitin ligase.
PMID: 18631453
IRAK2 leads to K63-linked polyubiquitination of TRAF6, which serves as a platform to recruit TAK1.
PMID: 18631453
IRAK1 has a similar role to IRAK2—it leads to K63-linked polyubiquitination of TRAF6 and TAK1 recruitment.
PMID: 18361453
TRAF6 is then thought to autoubiquinate, attaching K63-polyubiquitin to itself.
PMID: 18631453
IRAK2 leads to K63-linked polyubiquitination of TRAF6, which serves as a platform to recruit TAK1.
PMID: 18631453
IRAK1 has a similar role to IRAK2—it leads to K63-linked polyubiquitination of TRAF6 and TAK1 recruitment.
PMID: 18631453, 11057907
The E2-conjugating complexes Ubc13 and Uev1a are also involved in this process.
PMID: 18631453
K63-polyubiquitin-TRAF6 can then recruit TAK1 in a complex with TAB2 and TAB3, which both contain nuclear zinc-finger motifs that interact with K63-polyubiquitin chains.
PMID: 18631453
This somehow activates TAK1, which then couples to the IKK complex, which contains the scaffold protein NEMO and the kinase responsible for phosphorylation of I-kappaB, IKK2.
PMID: 18631453
This somehow activates TAK1, which then couples to the IKK complex, which contains the scaffold protein NEMO and the kinase responsible for phosphorylation of I-kappaB, IKK2.
Indirect
PMID: 18631453
This somehow activates TAK1, which then couples to the IKK complex, which contains the scaffold protein NEMO and the kinase responsible for phosphorylation of I-kappaB, IKK2.
PMID: 18631453
TAK1 also couples to MKK3-MKK6 and MKK7, the respective upstream kinases for p38 and JNK.
PMID: 18631453
TAK1 also couples to MKK3-MKK6 and MKK7, the respective upstream kinases for p38 and JNK.
Indirect
PMID: 18631453
These ultimately trigger NF-kappaB, p38, and ERK activation.
PMID: 18631453
It might involve activation of PI3 kinase, which via Akt has been shown to block NF-kappaB activation by TLR4.
PMID: 18631453, 18391954
It has been shown that SHP1 negatively regulates TLR-mediated production of proinflammatory cytokines by inhibiting activation of NF-kappaB and MAP kinases.
Indirect
PMID: 18631453
These ultimately trigger NF-kappaB, p38, and ERK activation.
PMID: 18631453, 18391954
It has been shown that SHP1 negatively regulates TLR-mediated production of proinflammatory cytokines by inhibiting activation of NF-kappaB and MAP kinases.
PMID: 18631453
MyD88 adaptor-like (Mal, also called TIRAP) is recruited by TLR2 and TLR4, and so far its main function appears to be to subsequently stabilize MyD88 in the complex, acting as a bridge.
PMID: 18631453, 18327267
A uropathogenic strain of E. coli, termed CFT073, was then shown to have a TIR-domain-containing protein termed TIR-containing protein C (TcpC). The bacteria release this protein, which is somehow taken up by macrophages, where it interacts with MyD88 to prevent signaling.
PMID: 18631453
MyD88 adaptor-like (Mal, also called TIRAP) is recruited by TLR2 and TLR4, and so far its main function appears to be to subsequently stabilize MyD88 in the complex, acting as a bridge.
PMID: 18631453, 18327267
A uropathogenic strain of E. coli, termed CFT073, was then shown to have a TIR-domain-containing protein termed TIR-containing protein C (TcpC). The bacteria release this protein, which is somehow taken up by macrophages, where it interacts with MyD88 to prevent signaling.
PMID: 18631453
Trif is used by TLR3 and also TLR4, but in the case of TLR4 another bridging adaptor is needed, Tram.
PMID: 18631453
TLR4 in endosomes recruits TRAM and TRIF, leading to TRAF3 activation.
PMID: 18631453
Trif is used by TLR3 and also TLR4, but in the case of TLR4 another bridging adaptor is needed, Tram.
PMID: 18631453
Trif is used by TLR3 and also TLR4, but in the case of TLR4 another bridging adaptor is needed, Tram.
PMID: 18631453
TLR4 in endosomes recruits TRAM and TRIF, leading to TRAF3 activation.
PMID: 18631453
TLR4 in endosomes recruits TRAM and TRIF, leading to TRAF3 activation.
PMID: 18631453, 18222170, 18297073
Trif leads to IRF3 activation via recruitment of the kinase TBK-1, and this signal, in the case of both TLR3 and TLR4, comes from the endosome, with TLR4 trafficking there after LPS recognition.
PMID: 18631453
In this case, SHP2 was shown to target TBK-1, the kinase that phosphorylates IRF3.
PMID: 18631453, 18356163
In addition, another study has shown that activation of TBK-1, the upstream kinase for IRF3, is inhibited by glucocorticoids, again pointing to a more general mechanism rather than inhibition of TLR4 specifically.
PMID: 18631453, 18222170, 18297073
Trif leads to IRF3 activation via recruitment of the kinase TBK-1, and this signal, in the case of both TLR3 and TLR4, comes from the endosome, with TLR4 trafficking there after LPS recognition.
PMID: 18631453
In this case, SHP2 was shown to target TBK-1, the kinase that phosphorylates IRF3.
PMID: 18631453
TLR4 will then traffic to endosomes, where TRAM is now engaged, recruiting TRIF, which in turn recruits TRAF3 to activate TBK-1.
PMID: 18631453, 18222170, 18297073
Trif leads to IRF3 activation via recruitment of the kinase TBK-1, and this signal, in the case of both TLR3 and TLR4, comes from the endosome, with TLR4 trafficking there after LPS recognition.
PMID: 18631453, 18222170, 18297073
Trif leads to IRF3 activation via recruitment of the kinase TBK-1, and this signal, in the case of both TLR3 and TLR4, comes from the endosome, with TLR4 trafficking there after LPS recognition.
PMID: 18631453, 16757566
Phosphorylation of TRAM on serine 16 by protein kinase C-epsilon is required for this process and may be required for endosomal trafficking or displacement of Mal-MyD88 from the complex.
PIMD: 18631453, 16751103, 16603631
Mal has a phosphatidylinositol-4,5-bisphosphase (PIP2) binding domain that localizes it to the plasma membrane, whereas TRAM is myristoylated for the same reason.
PIMD: 18631453, 16751103, 16603631
Mal has a phosphatidylinositol-4,5-bisphosphase (PIP2) binding domain that localizes it to the plasma membrane, whereas TRAM is myristoylated for the same reason.
Indirect
PIMD: 18631453, 16751103, 16603631
Mal has a phosphatidylinositol-4,5-bisphosphase (PIP2) binding domain that localizes it to the plasma membrane, whereas TRAM is myristoylated for the same reason.
PIMD: 18631453, 16751103, 16603631
Mal has a phosphatidylinositol-4,5-bisphosphase (PIP2) binding domain that localizes it to the plasma membrane, whereas TRAM is myristoylated for the same reason.
PMID: 18631453, 17724133
It has also been shown to be expressed in neurons, where it interacts with the MAP kinase JNK3.
PMID: 18631453, 18327267
A uropathogenic strain of E. coli, termed CFT073, was then shown to have a TIR-domain-containing protein termed TIR-containing protein C (TcpC). The bacteria release this protein, which is somehow taken up by macrophages, where it interacts with MyD88 to prevent signaling.
Indirect
PMID: 18631453
A clear-cut example of this “two-signal” approach is the ability of TLRs to induce pro-IL-1beta production, but without causing processing to the mature cytokine, as shown in Figure 1.
Indirect
PMID: 18631453
Various stimuli act via Nalp3 to activate caspase-1, which processes the pro-IL-1beta protein into mature IL-1beta.
PMID: 18631453, 15530394, 16407889, 18403674
Nalp3 is a key component of an important caspase-1-containing inflammasome and is activated by various pathogens; such substances as ATP, MDP and, most recently, other types of crystals such as asbestos and silica.
PMID: 18631453, 15530394, 16407889, 18403674
Nalp3 is a key component of an important caspase-1-containing inflammasome and is activated by various pathogens; such substances as ATP, MDP and, most recently, other types of crystals such as asbestos and silica.
Indirect
Indirect
PMID: 18631453, 17433728
The mechanism of Nalp3 activation has been shown to involve a potassium efflux, mediated by the P2X7 receptor in combination with the ion channel pannexin-1.
Indirect
Indirect
Indirect
PMID: 18631453, 17433728
The mechanism of Nalp3 activation has been shown to involve a potassium efflux, mediated by the P2X7 receptor in combination with the ion channel pannexin-1.
PMID: 18631453
It also appears to involve reactive oxygen species (ROS) generated by the NADPH oxidase, although how the potassium efflux or ROS generation leads to Nalp3 activation is not known.
Indirect
Indirect
PMID: 18631453
It also appears to involve reactive oxygen species (ROS) generated by the NADPH oxidase, although how the potassium efflux or ROS generation leads to Nalp3 activation is not known.
PMID: 18631453
Uric acid and asbestos have been shown to activate NADPH-oxidase-generating reactive oxygen species (ROS), which are also required for Nalp3 activation, although again a mechanism is missing.
Indirect
Indirect
PMID: 18631453
TLR ligands such as LPS or the TLR7 ligand R837 also modulate the inflammasome, enabling ATP to activate caspase-1 via Nalp3.
Indirect
Indirect
PMID: 18631453
TLR ligands such as LPS or the TLR7 ligand R837 also modulate the inflammasome, enabling ATP to activate caspase-1 via Nalp3.
PMID: 18631453
TLRs such as TLR4 and TLR7 activate the standard signaling pathway via MyD88 and NF-kappaB to induce pro-IL-1beta mRNA.
Indirect
PMID: 18631453
TLRs such as TLR4 and TLR7 activate the standard signaling pathway via MyD88 and NF-kappaB to induce pro-IL-1beta mRNA.
PMID: 18631453, 18391954
It has been shown that SHP1 negatively regulates TLR-mediated production of proinflammatory cytokines by inhibiting activation of NF-kappaB and MAP kinases.
Indirect
PMID: 18631453
TLRs such as TLR4 and TLR7 activate the standard signaling pathway via MyD88 and NF-kappaB to induce pro-IL-1beta mRNA.
Indirect
PMID: 18631453
TLR4 in the plasma membrane engages with Mal and subsequently MyD88, for NF-kappaB activation via TRAF6.
Indirect
PMID: 18631453
TLR4 in the plasma membrane engages with Mal and subsequently MyD88, for NF-kappaB activation via TRAF6.
PMID: 18631453
It might involve activation of PI3 kinase, which via Akt has been shown to block NF-kappaB activation by TLR4.
Indirect
PMID: 18631453
Various stimuli act via Nalp3 to activate caspase-1, which processes the pro-IL-1beta protein into mature IL-1beta. These stimuli include ATP, MDP, uric acid, and asbestos.
Indirect
PMID: 18631453
Various stimuli act via Nalp3 to activate caspase-1, which processes the pro-IL-1beta protein into mature IL-1beta. These stimuli include ATP, MDP, uric acid, and asbestos.
Indirect
PMID: 18631453
Various stimuli act via Nalp3 to activate caspase-1, which processes the pro-IL-1beta protein into mature IL-1beta. These stimuli include ATP, MDP, uric acid, and asbestos.
Indirect
Indirect
PMID: 18631453
It also appears to involve reactive oxygen species (ROS) generated by the NADPH oxidase, although how the potassium efflux or ROS generation leads to Nalp3 activation is not known.
PMID: 18631453
Uric acid and asbestos have been shown to activate NADPH-oxidase-generating reactive oxygen species (ROS), which are also required for Nalp3 activation, although again a mechanism is missing.
Indirect
PMID: 18631453
TAM receptors in a complex with IFNAR1 induce SOCS1, which inhibits TLR4 by targeting Mal, and SOCS3, which inhibits TRAF3 and TRAF6.
Indirect
PMID: 18631453, 9151903
Notably, the tyrosine kinases Src, Hck, and Lyn have been shown to be activated by TLR4, although their exact role is uncertain because a hck, fyn, lyn triple-deficient mouse was normal for TLR4 signaling.
Indirect
PMID: 18631453, 9151903
Notably, the tyrosine kinases Src, Hck, and Lyn have been shown to be activated by TLR4, although their exact role is uncertain because a hck, fyn, lyn triple-deficient mouse was normal for TLR4 signaling.
Indirect
PMID: 18631453, 9151903
Notably, the tyrosine kinases Src, Hck, and Lyn have been shown to be activated by TLR4, although their exact role is uncertain because a hck, fyn, lyn triple-deficient mouse was normal for TLR4 signaling.
PMID: 18631453, 15849198, 17932028, 18276597
Btk is recruited to both TLR4 and TLR9 and has been shown to be involved in the pathway leading to enhanced phosphorylation of the p65 subunit of NF-kappaB on serine 536, which is required for p65 to promote gene expression.
PMID: 18631453, 15849198, 17932028, 18276597
Btk is recruited to both TLR4 and TLR9 and has been shown to be involved in the pathway leading to enhanced phosphorylation of the p65 subunit of NF-kappaB on serine 536, which is required for p65 to promote gene expression.
Indirect
PMID: 18631453, 15849198, 17932028, 18276597
Btk is recruited to both TLR4 and TLR9 and has been shown to be involved in the pathway leading to enhanced phosphorylation of the p65 subunit of NF-kappaB on serine 536, which is required for p65 to promote gene expression.
Indirect
PMID: 18631453, 15849198, 17932028, 18276597
Btk is recruited to both TLR4 and TLR9 and has been shown to be involved in the pathway leading to enhanced phosphorylation of the p65 subunit of NF-kappaB on serine 536, which is required for p65 to promote gene expression.
Indirect
PMID: 18631453, 18276597
In B cells, Btk is required for TLR9-induced proliferation and IL-10 production.
Indirect
Indirect
PMID: 18631453, 18276597
In B cells, Btk is required for TLR9-induced proliferation and IL-10 production.
Indirect
Indirect
PMID: 18631453, 17082638
Btk is also required for IL-10 induction by TLR4 in macrophages.
Indirect
PMID: 18631453, 16439361, 18070880
One substrate is Mal, which undergoes phosphorylation by Btk on Tyr-86 and Tyr-106.
PMID: 18631453, 16415872
This event is required for Mal to signal NF-kappaB activation but, in addition, is involved in the ultimate degradation of Mal via the recruitment of suppressor of cytokine signaling 1 (SOCS1).
PMID: 18631453, 16415872
This event is required for Mal to signal NF-kappaB activation but, in addition, is involved in the ultimate degradation of Mal via the recruitment of suppressor of cytokine signaling 1 (SOCS1).
Indirect
PMID: 18631453
The tyrosine kinase Syk plays a key role in DAP12 activation, phosphorylating tyrosine residues, and allowing for the recruitment of SH2-domain-containing proteins such as the p85-p110 dimer of PI3 kinase and phospholipase Cgamma.
PMID: 18631453
The tyrosine kinase Syk plays a key role in DAP12 activation, phosphorylating tyrosine residues, and allowing for the recruitment of SH2-domain-containing proteins such as the p85-p110 dimer of PI3 kinase and phospholipase Cgamma.
PMID: 18631453
The tyrosine kinase Syk plays a key role in DAP12 activation, phosphorylating tyrosine residues, and allowing for the recruitment of SH2-domain-containing proteins such as the p85-p110 dimer of PI3 kinase and phospholipase Cgamma.
Indirect
Indirect
PMID: 1831453
At first, this seemed counterintuitive, because ITAM-containing proteins that couple to receptors had been shown to activate signaling pathways leading to inflammatory cytokine production, such as DAP12, which couples to the coreceptor TREM-1.
PMID: 18631453
The effect here appears to be proximity dependent—the antibody binds to TLR4 and the Fc portion binds to CD32A, bringing it into close proximity to TLR4.
PMID: 18631453
The effect here appears to be proximity dependent—the antibody binds to TLR4 and the Fc portion binds to CD32A, bringing it into close proximity to TLR4.
Indirect
PMID: 18631453
It might involve activation of PI3 kinase, which via Akt has been shown to block NF-kappaB activation by TLR4.
PMID: 18631453
It might involve activation of PI3 kinase, which via Akt has been shown to block NF-kappaB activation by TLR4.
Indirect
PMID: 18631453
Alternatively, because CD32A can activate phospholipase C-gamma, a depletion in PIP2 by this enzyme might lead to Mal's dissociation from the plasma membrane.
PMID: 18631453
Alternatively, because CD32A can activate phospholipase C-gamma, a depletion in PIP2 by this enzyme might lead to Mal's dissociation from the plasma membrane.
Indirect
PMID: 18631453
Alternatively, because CD32A can activate phospholipase C-gamma, a depletion in PIP2 by this enzyme might lead to Mal's dissociation from the plasma membrane.
PMID: 18631453
Gas6 binds all three, although with different affinities.
PMID: 18631453
The ligands for the TAM receptors Gas6 and Protein S activate a signaling pathway via the R1 subunit of the type I interferon receptor, which has been shown to occur in a complex with Axl.
Indirect
PMID: 18631453
This leads to activation of STAT1 and, in turn, induction of SOCS1 and SOCS3, which act to block TLR signaling.
Indirect
PMID: 18631453
This leads to activation of STAT1 and, in turn, induction of SOCS1 and SOCS3, which act to block TLR signaling.
Indirect
PMID: 18631453
This leads to activation of STAT1 and, in turn, induction of SOCS1 and SOCS3, which act to block TLR signaling.
PMID: 18631453
The mechanism in both cases appears to be SHP1 binding to the kinase domain of IRAK-1 (which contains several phosphoaccepting tyrosines), where it inhibits its activity.
PMID: 18631453, 18391954
This kinase activity is required for induction of proinflammatory cytokines, but is somehow inhibitory for induction of type I interferons, because autophosphoylation of IRAK1 leads to its degradation, allowing for increased production of type I interferons.
Indirect
PMID: 18631453, 18391954
This kinase activity is required for induction of proinflammatory cytokines, but is somehow inhibitory for induction of type I interferons, because autophosphoylation of IRAK1 leads to its degradation, allowing for increased production of type I interferons.
PMID: 18631453, 18391954
This kinase activity is required for induction of proinflammatory cytokines, but is somehow inhibitory for induction of type I interferons, because autophosphoylation of IRAK1 leads to its degradation, allowing for increased production of type I interferons.
Indirect
Indirect
PMID: 18631453
Intriguingly, SHP1 promotes production of type I interferons by TLRs and also RIG-I.
Indirect
Indirect
Indirect
PMID: 18631453
Intriguingly, SHP1 promotes production of type I interferons by TLRs and also RIG-I.
Indirect
PMID: 18631453
In this case, SHP2 was shown to target TBK-1, the kinase that phosphorylates IRF3.
Indirect
PMID: 18631453
In this case, SHP2 was shown to target TBK-1, the kinase that phosphorylates IRF3.
Indirect
Indirect
PMID: 18631453
Although related, therefore, SHP1 and SHP2 have opposite effects. SHP1 promotes interferon-β production in response to TLRs, whereas SHP2 is inhibitory.
Indirect
PMID: 18631453
SHP2 limits TLR3-induced production of proinflammatory cytokines and interferon-beta, without affecting TLR2 or TLR9 signaling.
Indirect
PMID: 18631453
SHP2 limits TLR3-induced production of proinflammatory cytokines and interferon-beta, without affecting TLR2 or TLR9 signaling.
PMID: 18631453
In IL-1 signaling, MyD88 is recruited to the receptor complex within seconds, where it stably associates.
PMID: 18631453
For TLR3, IRAK2 is directly recruited.
PMID: 18631453
It was shown that similar to IRAK1, IRAK2 was activated downstream of IRAK4.
Indirect
PMID: 18631453
A20 is a key ubiquitin-editing enzyme that restricts TLR responses by regulating the ubiquitination of key signaling proteins such as Traf6.
pMID: 18631453, 17675297, 17997719
Two proteins, termed Pellino-1 and Pellino-3b, appear to be important in this process. These proteins were known to interact with IRAK-1, and recent studies indicate that similar to Traf6, they are E3 ligases.
PMID: 18631453
Importantly, their activity is greatly enhanced, at least in vitro, in response to phosphorylation by IRAK1 and IRAK4.
PMID: 18631453
The role of the kinase activity of IRAK1 and/or IRAK4 might therefore be at least initially to activate Pellinos, such that they can cause K63-linked polyubiquitination of IRAK1.
PMID: 18631453
Most interestingly, this recruits NEMO to IRAK1, with NEMO binding to polyubiquitin.
Indirect
PMID: 18631453
These ultimately trigger NF-kappaB, p38, and ERK activation.
PMID: 18631453, 18391954
It has been shown that SHP1 negatively regulates TLR-mediated production of proinflammatory cytokines by inhibiting activation of NF-kappaB and MAP kinases.
PMID: 18631453
Ultimately, both IRAK1 and the Pellinos (which also undergo ubiquitination) are probably degraded to terminate the signal.
PMID: 18631453
There is also evidence that TRAF6 ubiquitinates IRAK1.
PMID: 18631453, 18345001
In the second study, a protein termed TRIM30-alpha, which has a RING finger (often indicative of E3 ubiquitin ligase activity) was shown to limit TLR signaling by targeting TAB2 and TAB3, causing their degradation. This effect was not via the ubiquitin-proteasome pathway, however, but depended on lysosomal degradation.
PMID: 18631453, 18345001
In the second study, a protein termed TRIM30-alpha, which has a RING finger (often indicative of E3 ubiquitin ligase activity) was shown to limit TLR signaling by targeting TAB2 and TAB3, causing their degradation. This effect was not via the ubiquitin-proteasome pathway, however, but depended on lysosomal degradation.
Indirect
PMID: 18631453, 12391149, 16880258, 16380513
The mechanism was shown to involve induction of a phosphatase termed MKP-1 which dephosphorylates p38 and thereby inactivates it.
Indirect
PMID: 18631453
There is a role in TNF production, however, which was shown to be due to Btk's being required for p38 activation, which then stabilizes TNF but not IL-6 mRNA.
Indirect
PMID: 18631453, 12391149, 16880258, 16380513
The mechanism was shown to involve induction of a phosphatase termed MKP-1 which dephosphorylates p38 and thereby inactivates it.
PMID: 18631453
GRIP1 is a protein that interacts with the glucocorticoid receptor.
PMID: 18631453
A yeast two-hybrid screen isolated IRF3 as an interacting protein, and it was shown that GRIP1 was required for IRF3-mediated transactivation.
PMID: 18631453, 16362036
Importantly the glucocorticoid receptor competed with IRF3 for GRIP1 and thereby blocked IRF3-mediated gene expression.
Indirect
PMID: 18631453, 16362036
Importantly the glucocorticoid receptor competed with IRF3 for GRIP1 and thereby blocked IRF3-mediated gene expression.
Indirect
PMID: 18631453, 18345001
In the second study, a protein termed TRIM30-alpha, which has a RING finger (often indicative of E3 ubiquitin ligase activity) was shown to limit TLR signaling by targeting TAB2 and TAB3, causing their degradation.
Indirect
PMID: 18631453, 18345001
In the second study, a protein termed TRIM30-alpha, which has a RING finger (often indicative of E3 ubiquitin ligase activity) was shown to limit TLR signaling by targeting TAB2 and TAB3, causing their degradation.