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Indirect
PMID: 15662540
Activation of the IKK complex involves the phosphorylation of two serine residues located in the activation loop within the kinase domain of IKKα (S176 and S180) or IKKβ (S177 and S181).
PMID: 15662540
Once activated, TAK1 can directly phosphorylate IKKβ and mitogen-activated protein kinase kinase 6.
PMID: 15662540
TRAF6-TAK1-TAB2 are then translocated to the cytosol, where TAK1 is phosphorylated and activated, leading to the activation of IKK and NFκB.
Indirect
Indirect
PMID: 15662540
The IKKα and IKKβ subunits preferentially form heterodimers, and both can directly phosphorylate the critical S32 and S36 residues of IκBα.
PMID: 15662540
LPS-induced IκB and p38 phosphorylation are upregulated in SOCS1- deficient macrophages. Moreover, forced expression of SOCS1 suppresses LPS-induced NFκB activation.
PMID: 15662540
Phospho-IκB is then recognized by the β-transducin repeat containing protein containing Skp1/Cullin/F-box ubiquitin ligase complex, leading to its ubiquitination and degradation by the proteasome.
PMID: 15662540
Phospho-IκB is then recognized by the β-transducin repeat containing protein containing Skp1/Cullin/F-box ubiquitin ligase complex, leading to its ubiquitination and degradation by the proteasome.
PMID: 15662540, 10837071, 10713156
The destruction of IκB unmasks the nuclear localization signal of NFκB, leading to its nuclear translocation and binding to the promoters of target genes.
PMID: 15662540
The Ig domain subgroup includes IL-1 receptor (IL-1R) 1.
PMID: 15662540
Upon IL-1 stimulation adapter molecule MyD88 is first recruited to the IL-1 receptor.
PMID: 15662540, 11960013, 8599092
Upon IL-1 stimulation adapter molecule MyD88 is first recruited to the IL-1 receptor, followed by the recruitment of two serine-threonine kinases, IRAK4 and IRAK.
PMID: 15662540, 8837778
Upon IL-1 stimulation adapter molecule MyD88 is first recruited to the IL-1 receptor, followed by the recruitment of two serine-threonine kinases, IRAK4 and IRAK and the adapter TNF receptor associated factor (TRAF) 6.
PMID: 15662540
During the formation of Complex I IRAK4 is activated, leading to the hyperphosphorylation of IRAK.
PMID: 15662540
Unlike MyD88, MyD88s does not bind IRAK4, and overexpression of MyD88s does not induce IRAK phosphorylation.
PMID: 15662540, 12496252
During the formation of Complex I IRAK4 is activated, leading to the hyperphosphorylation of IRAK, which creates an interface for its interaction with adapter Pellino 1.
PMID: 15662540
The formation of Pellino 1-IRAK4-IRAKTRAF6 causes conformational changes in the receptor complex (Complex I), releasing these signaling molecules from the receptor.
PMID: 15662540
IRAKM prevents the dissociation of the IRAK-IRAK4 from MyD88 thereby inhibiting the formation of the IRAK-TRAF6 interaction.
PMID: 15662540
The released components then interact with the membrane-bound preassociated transforming growth factor β activated kinase (TAK) 1–transforming growth factor β activated protein kinase 1 binding protein (TAB) 1–TAB2 [28], resulting in the formation of Complex II (IRAK-TRAF6-TAK1-TAB1-TAB2).
PMID: 15662540
TAK1 and TAB2 are phosphorylated in the membrane-bound Complex II.
PMID: 15662540
TAK1 and TAB2 are phosphorylated in the membrane-bound Complex II, triggering the dissociation and translocation of TRAF6-TAK1-TAB1-TAB2 (Complex III) from the membrane to the cytosol.
PMID: 15662540
The translocated Complex III interacts with additional factors in the cytosol, leading to TAK1 activation.
PMID: 15662540
The activation of TAK1 eventually leads to the activation of IKK.
PMID: 15662540
Furthermore, it was shown that the TAK1 complex (TAK1-TAB1-TAB2) is activated by association with ubiquitinated TRAF6.
Indirect
PMID: 15662540
Once activated, TAK1 can directly phosphorylate IKKβ and mitogen-activated protein kinase kinase 6, leading to the activation of both the c-Jun N-terminal kinase and NFκB signaling pathways.
Indirect
PMID: 15662540
Activated TAK1 has also been implicated in the IL-1 induced activation of mitogen-activated protein kinase kinase 6 and c-Jun N-terminal kinase [46], leading to the activation of other transcription factors, including activating transcription factor and activator protein 1.
Indirect
PMID: 15662540
Activated TAK1 has also been implicated in the IL-1 induced activation of mitogen-activated protein kinase kinase 6 and c-Jun N-terminal kinase [46], leading to the activation of other transcription factors, including activating transcription factor and activator protein 1.
PMID: 15662540
TRAF6 functions as part of a unique E3 complex, with Ubc13 and Uev1A, and TRAF6 itself is the target of ubiquitination.
PMID: 15662540
TRAF6 functions as part of a unique E3 complex, with Ubc13 and Uev1A, and TRAF6 itself is the target of ubiquitination.
Indirect
PMID: 15662540
Once activated, TAK1 can directly phosphorylate IKKβ and mitogen-activated protein kinase kinase 6.
PMID: 15662540
It has been shown that MEKK3 forms a complex with TRAF6 in response to IL-1 and is crucial for IL-1 induced NFκB activation.
PMID: 15662540, 11607032
TLR3 recognizes doublestranded RNA (dsRNA).
PMID: 15662540, 12872135, 12855817
TRIF was recently identified as an adapter for TLR3.
PMID: 15662540
adapter molecule TRIF recruits TRAF6–TAK1–TAB2 to TLR3 through its TRAF6-binding site.
PMID: 15662540
receptor interacting protein (RIP) 1 has also been implicated in TLR3/TRIFmediated NFκB activation.
Indirect
PMID: 15662540
it is possible that RIP1 directly cooperates with the TRAF6-containing complex, facilitating the NFκB activation process.
PMID: 15662540
When over expressed, IRAK2a and IRAK2b potentiate NFκB activation by LPS. Interestingly, IRAK2c and IRAK2d were inhibitory.
PMID; 15662540
TRIF leads to the activation of TBK1/IKKε, resulting in IRF3 activation.
PMID:15662540, 12925853
The fact that SIGIRR forms a complex with the IL-1 receptor, IRAK, and TRAF6 upon IL-1 stimulation suggests that SIGIRR functions through its interaction with the TIR complex.
PMID: 15662540
Overexpression of ST2 was found to inhibit NFκB activation because ST2 associated with, and probably sequestered, MyD88 and TIRAP.Overexpression of ST2 was found to inhibit NFκB activation because ST2 associated with, and probably sequestered, MyD88 and TIRAP.
Indirect
PMID: 15662540
When over expressed, IRAK2a and IRAK2b potentiate NFκB activation by LPS. Interestingly, IRAK2c and IRAK2d were inhibitory.
Indirect
PMID: 15662540
When over expressed, IRAK2a and IRAK2b potentiate NFκB activation by LPS. Interestingly, IRAK2c and IRAK2d were inhibitory.
Indirect
PMID: 15662540
LPS induces the expression of IRAK2c.
PMID: 15662540
LPS induces the expression of IRAK2c.
PMID: 15662540
MyD88 forms homodimers through DD-DD and TIR-TIR domain interactions and exists as a dimer when recruited to the receptor complex.
PMID: 15662540
Unlike MyD88, MyD88s does not bind IRAK4, and overexpression of MyD88s does not induce IRAK phosphorylation.
Indirect
PMID: 15662540
MyD88s is induced in monocytes upon LPS stimulation.
PMID: 15662540
MyD88s is induced in monocytes upon LPS stimulation.
Indirect
PMID: 15662540
LPS induces the expression of SOCS1 in macrophages.
PMID: 15662540
LPS induces the expression of SOCS1 in macrophages.
Indirect
PMID: 15662540
LPS-induced NO2− synthesis and tumor necrosis factor α production are augmented in SOCS1- deficient macrophages.
PMID: 15662540
LPS-induced NO2− synthesis and tumor necrosis factor α production are augmented in SOCS1- deficient macrophages.
Indirect
PMID: 15662540
LPS-induced NO2− synthesis and tumor necrosis factor α production are augmented in SOCS1- deficient macrophages.
Indirect
PMID: 15662540
LPS-induced IκB and p38 phosphorylation are upregulated in SOCS1- deficient macrophages.
PMID: 15662540
In an initial step the ubiquitin-activating enzyme (E1 or Uba) forms a thioester bond with the C-terminus of ubiquitin.
PMID:15662540
In the final step the E2 enzyme donates ubiquitin to a lysine residue of the target protein, either directly or with the assistance of ubiquitin protein ligase (E3 or Ubr).
Indirect
PMID: 15662540
Triad3A overexpression promoted substantial degradation of TLR4 and TLR9.
Indirect
PMID:15662540
In the final step the E2 enzyme donates ubiquitin to a lysine residue of the target protein, either directly or with the assistance of ubiquitin protein ligase (E3 or Ubr).
Indirect
PMID: 15662540
Triad3A overexpression promoted substantial degradation of TLR4 and TLR9.
PMID: 15662540
Triad3A overexpression promoted substantial degradation of TLR4 and TLR9.
PMID: 15662540
Triad3A overexpression promoted substantial degradation of TLR4 and TLR9.
PMID: 15662540
TRAF6-TAK1-TAB2 are then translocated to the cytosol.
PMID: 15662540
TRAF6-TAK1-TAB2 are then translocated to the cytosol, where TAK1 is phosphorylated and activated.
PMID: 15662540, 11095740
TLR6 associates with TLR2 and recognizes lipoproteins from microplasma.
PMID: 15662540, 11095740
TLR6 associates with TLR2 and recognizes lipoproteins from microplasma.
PMID: 15662540, 11323673
While TLR5 mediates the induction of the immune response by bacterial flagellins.
PMID: 15662540, 11130078
TLR9 has been shown to recognize bacterial DNA.
PMID: 15662540, 11812998, 10346978
While a synthetic compound (imidazoquinoline compound R848) with antiviral activity has been described as a ligand for TLR7 and TLR8.
11812998, 10346978
While a synthetic compound (imidazoquinoline compound R848) with antiviral activity has been described as a ligand for TLR7 and TLR8.
PMID: 15662540, 14976261, 14976262, 15034168
recent studies showed that ssRNA is the natural ligand for TLR7/8.
PMID: 15662540, 14976261, 14976262, 15034168
recent studies showed that ssRNA is the natural ligand for TLR7/8.
Indirect
PMID: 15662540
It has been shown that MEKK3 forms a complex with TRAF6 in response to IL-1 and is crucial for IL-1 induced NFκB activation.
PMID; 15662540
TRIF leads to the activation of TBK1/IKKε, resulting in IRF3 activation.
PMID: 15662540
Viral infection and Toll ligands (dsRNA and LPS) lead to the phosphorylation of IRF3 and its subsequent dimerization.
PMID: 15662540
Viral infection and Toll ligands (dsRNA and LPS) lead to the phosphorylation of IRF3 and its subsequent dimerization.
PMID: 15662540
Viral infection and Toll ligands (dsRNA and LPS) lead to the phosphorylation of IRF3 and its subsequent dimerization and interaction with the coactivaotors cAMP-response element binding protein binding protein and p300.
PMID: 15662540
The IRF3 complex then translocates to the nucleus.
PMID: 15662540
The IRF3 complex then translocates to the nucleus, where it activates promoters containing IRF-binding sites.
PMID: 15662540, 10435584
TLR4-mediated NFκB activation was greatly reduced in MyD88- deficient mice, indicating the requirement of MyD88 for TLR4 signaling.
PMID: 15662540, 12447442, 12447441
Interestingly, TIRAP-deficient mice showed defects in activation of the MyD88-dependent signaling pathway through TLR4, but not IL-1R, indicating specificity of the TLR4-mediated MyD88-dependent pathway.
PMID: 15662540
LPS-induced, TLR4-mediated signaling employs multiple TIR-domain containing adaptors, MyD88/TIRAP to mediate NFκB activation.
PMID: 15662540, 12855817
Such TLR4-mediated MyD88-independent activities were abolished in TRIF-deficient mice.
PMID: 15662540
TLR4- but not TLR3-mediated MyD88-independent IRF3 activation and interferon β production was abolished in TRAM-deficient mice.
PMID: 15662540
LPS still stimulates the expression of certain genes, including interferon β, in MyD88- deficient mice.
PMID: 15662540
Recently the IKK-related kinases IKKε and TRAF family member associated NFκB activator binding kinase binding kinase 1 have been implicated in the phosphorylation and activation of IRF3.
PMID: 15662540
LPS-induced, TLR4-mediated signaling employs multiple TIR-domain containing adaptors, MyD88/TIRAP to mediate NFκB activation, TRIF/TRAM for IRF3 activation.
PMID: 15662540
In an initial step the ubiquitin-activating enzyme (E1 or Uba) forms a thioester bond with the C-terminus of ubiquitin, which is then transferred to a specific cysteine residue of an ubiquitinconjugating enzyme (E2 or Ubc).
PMID: 15662540
Viral infection and Toll ligands (dsRNA and LPS) lead to the phosphorylation of IRF3 and its subsequent dimerization and interaction with the coactivaotors cAMP-response element binding protein binding protein and p300.
PMID: 15662540
The IRF3 complex then translocates to the nucleus, where it activates promoters containing IRF-binding sites.
PMID: 15662540
The IRF3 complex then translocates to the nucleus.
PMID: 15662540
Activation of the IKK complex involves the phosphorylation of two serine residues located in the activation loop within the kinase domain of IKKα (S176 and S180) or IKKβ (S177 and S181).
PMID: 15662540
Once activated, TAK1 can directly phosphorylate IKKβ and mitogen-activated protein kinase kinase 6.
PMID: 15662540
TRAF6-TAK1-TAB2 are then translocated to the cytosol, where TAK1 is phosphorylated and activated, leading to the activation of IKK and NFκB.