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PMID: 16698941
lipopolysaccharides (LPS) from Gram-negative bacteria are recognized by TLR4.
PMID: 16698941
TLR2, in combination with TLR1 or TLR6, recognizes triacyl lipopeptides and diacyl lipopeptides, respectively
PMID: 16698941
TLR2, in combination with TLR1 or TLR6, recognizes triacyl lipopeptides and diacyl lipopeptides, respectively
PMID: 16698941
TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, and single-stranded (ss)RNA derived from viruses such as human immunodeficiency virus.
PMID: 16698941
TLR3 recognizes double-stranded (ds)RNA, which is produced from many viruses during replication.
PMID: 16698941
TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, and single-stranded (ss)RNA derived from viruses such as human immunodeficiency virus.
PMID: 16698941
TLR7 recognizes synthetic imidazoquinoline-like molecules, guanosine analogs such as loxoribine, and single-stranded (ss)RNA derived from viruses such as human immunodeficiency virus.
PMID: 16698941
TLR8 mediates the recognition of imidazoquinolines and ssRNA.
PMID: 16698941
TLR8 mediates the recognition of imidazoquinolines and ssRNA.
PMID: 16698941
TLR9 recognizes bacterial and viral CpG DNA motifs.
PMID: 16698941, 15001781
TLR5 recognizes flagellin, and human TLR11 recognizes uropathogenic Escherichia coli.
PMID: 16698941, 16111920, 15860593
The first defined ligand for TLR11 has been described in mice as a profilin-like protein, a class of actin-binding proteins present in apicomplexan protozoa.
indirect
PMID: 16698941
In addition, antiviral type I interferons (IFNs; IFN-ß and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
indirect
PMID: 16698941
In addition, antiviral type I interferons (IFNs; IFN-ß and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
indirect
PMID: 16698941
In addition, antiviral type I interferons (IFNs; IFN-ß and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
indirect
PMID: 16698941
In addition, antiviral type I interferons (IFNs; IFN-ß and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
indirect
PMID: 16698941
In addition, antiviral type I interferons (IFNs; IFN-ß and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
indirect
PMID: 16698941
In addition, antiviral type I interferons (IFNs; IFN-ß and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
indirect
PMID: 16698941
In addition, antiviral type I interferons (IFNs; IFN-ß and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
indirect
PMID: 16698941
In addition, antiviral type I interferons (IFNs; IFN-ß and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
indirect
PMID: 16698941
In addition, antiviral type I interferons (IFNs; IFN-ß and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
indirect
PMID: 16698941
In addition, antiviral type I interferons (IFNs; IFN-ß and multiple IFN-{alpha}) are induced by TLR3, -4, -7, -8, and -9.
PMID: 16698941, 16474426, 15208624
viral-derived dsRNA may also be recognized by the cytosolic RNA helicase retinoic acid-inducible gene-I, inducing type I IFN in a TLR-independent manner.
indirect
PMID: 16698941, 16474426, 15208624
viral-derived dsRNA may also be recognized by the cytosolic RNA helicase retinoic acid-inducible gene-I, inducing type I IFN in a TLR-independent manner.
PMID: 16698941, 15107846
TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
PMID: 16698941, 15107846
TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
PMID: 16698941, 15107846
TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
PMID: 16698941, 15107846
TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
PMID: 16698941, 15107846
TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
PMID: 16698941, 15107846
TRIAD3A was a molecule found to bind the cytoplasmic domain of TLR4 and TLR9, but not TLR2, and to promote the ubiquitination and degradation of TLR4 and TLR9, but not TLR2.
PMID: 16698941, 15004187
Transforming growth factor-ß (TGF-ß) suppresses the expression of TLR4
PMID: 16698941, 15004187
Transforming growth factor-ß (TGF-ß) suppresses the expression of TLR4
indirect
PMID: 16698941, 15107846
overexpression of TRIAD3A reduced TLR4- and TLR9-mediated nuclear factor (NF)-{kappa}B activation in response to L and CpG but not pI:C
indirect
PMID: 16698941, 15107846
overexpression of TRIAD3A reduced TLR4- and TLR9-mediated nuclear factor (NF)-{kappa}B activation in response to L and CpG but not pI:C
PMID: 16698941, 16410796
Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
PMID: 16698941, 16410796
Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
PMID: 16698941, 16410796
Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
PMID: 16698941, 16410796
Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
PMID: 16698941, 16410796
Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
PMID: 16698941, 16410796
Mal acts as a bridging adaptor between TLR4, TLR1/2, TLR2/6, and MyD88.
PMID: 16698941, 12471095
Trif interacts directly with TLR3.
PMID: 16698941, 14556004
Tram is thought to act as a bridging adaptor between Trif and TLR4.
PMID: 16698941, 14556004
Tram is thought to act as a bridging adaptor between Trif and TLR4.
PMID: 16698941
MyD88 recruits IL-1R-associated kinase 4 (IRAK4) and TNF receptor-associated factor 6 (TRAF6) upon ligand stimulation.
PMID: 16698941
Upon activation of TLR signaling, IRAK-1 and IRAK-4 are recruited to the receptor complex.
PMID: 16698941
At the receptor, IRAK-1 associates with Toll-interacting protein (Tollip), MyD88, and TRAF6, and phosphorylation by IRAK-4 triggers IRAK-1 hyperphosphorylation and dissociation of IRAK-1 from the complex while still maintaining its engagement with TRAF6.
PMID: 16698941
At the receptor, IRAK-1 associates with Toll-interacting protein (Tollip), MyD88, and TRAF6, and phosphorylation by IRAK-4 triggers IRAK-1 hyperphosphorylation and dissociation of IRAK-1 from the complex while still maintaining its engagement with TRAF6.
PMID: 16698941, 12885415
MyD88s inhibits the ability of IRAK4 to phosphorylate IRAK1, as unlike full-length MyD88, it is unable to interact with IRAK4.
PMID: 16698941
At the receptor, IRAK-1 associates with Toll-interacting protein (Tollip), MyD88, and TRAF6, and phosphorylation by IRAK-4 triggers IRAK-1 hyperphosphorylation and dissociation of IRAK-1 from the complex while still maintaining its engagement with TRAF6.
PMID: 16698941
Tollip interacts with IRAK-1, and IRAK-1 autophosphorylation is suppressed in the presence of Tollip.
PMID: 16698941, 11751856
Following TLR stimulation, IRAK-1 phosphorylates Tollip, and this may lead to the release of Tollip from the Tollip:IRAK-1 complex, thus overcoming negative regulation.
PMID: 16698941
At the receptor, IRAK-1 associates with Toll-interacting protein (Tollip), MyD88, and TRAF6, and phosphorylation by IRAK-4 triggers IRAK-1 hyperphosphorylation and dissociation of IRAK-1 from the complex while still maintaining its engagement with TRAF6.
PMID: 16698941, 11751856
Following TLR stimulation, IRAK-1 phosphorylates Tollip, and this may lead to the release of Tollip from the Tollip:IRAK-1 complex, thus overcoming negative regulation
PMID: 16698941
IRAK then becomes phosphorylated and dissociates from MyD88, which results in TRAF6 being activated, followed by TAK1/TAB1/TAB2/TAB3 complex formation and activation via K63-linked ubiquitination.
PMID: 16698941
IRAK then becomes phosphorylated and dissociates from MyD88, which results in TRAF6 being activated, followed by TAK1/TAB1/TAB2/TAB3 complex formation and activation via K63-linked ubiquitination.
indirect
PMID: 16698941
IRAK then becomes phosphorylated and dissociates from MyD88, which results in TRAF6 being activated, followed by TAK1/TAB1/TAB2/TAB3 complex formation and activation via K63-linked ubiquitination.
indirect
PMID: 16698941
Activated TAK1 complex then activates the inhibitor of {kappa}B (I{kappa}B) kinase (IKK) complex, which catalyzes I{kappa}B phosphorylation and degradation by the proteasome pathway, thus allowing NF-{kappa}B to translocate into nuclei.
PMID: 16698941
Activated TAK1 complex then activates the inhibitor of {kappa}B (I{kappa}B) kinase (IKK) complex, which catalyzes I{kappa}B phosphorylation and degradation by the proteasome pathway, thus allowing NF-{kappa}B to translocate into nuclei.
PMID: 16698941
Activated TAK1 complex then activates the inhibitor of {kappa}B (I{kappa}B) kinase (IKK) complex, which catalyzes I{kappa}B phosphorylation and degradation by the proteasome pathway, thus allowing NF-{kappa}B to translocate into nuclei.
PMID: 16698941
Activated TAK1 complex then activates the inhibitor of {kappa}B (I{kappa}B) kinase (IKK) complex, which catalyzes I{kappa}B phosphorylation and degradation by the proteasome pathway, thus allowing NF-{kappa}B to translocate into nuclei.
PMID: 16698941
TLR4 also recruits TRAM and Trif, which interacts with Traf family member-associated NF-{kappa}B activator-binding protein (TBK1), and TBK1, together with inducible IKK (IKKi), mediates phosphorylation of IFN regulatory factor 3 (IRF3).
PMID: 16698941
TLR4 also recruits TRAM and Trif, which interacts with Traf family member-associated NF-{kappa}B activator-binding protein (TBK1), and TBK1, together with inducible IKK (IKKi), mediates phosphorylation of IFN regulatory factor 3 (IRF3).
PMID: 16698941
Phosphorylated IRF3 is dimerized and translocated into the nucleus to bind DNA.
PMID: 16698941
Phosphorylated IRF3 is dimerized and translocated into the nucleus to bind DNA.
PMID: 16698941
Phosphorylated IRF3 is dimerized and translocated into the nucleus to bind DNA.
PMID: 16698941
Trif also interacts with TRAF6 and receptor-interacting protein kinase 1 (RIP1), which mediate NF-{kappa}B activation.
indirect
PMID: 16698941
Trif also interacts with TRAF6 and receptor-interacting protein kinase 1 (RIP1), which mediate NF-{kappa}B activation.
PMID: 16698941, 15247281
Mal interacts directly with TRAF6 to mediate NF-{kappa}B activation through TLR2 and TLR4.
PMID: 16698941, 14530355
Trif was found to mediate TLR3-induced activation of NF-{kappa}B via association with TRAF6.
indirect
PMID: 16698941, 14530355
Trif was found to mediate TLR3-induced activation of NF-{kappa}B via association with TRAF6.
PMID: 16698941
it was shown that TRAF1 is cleaved by caspase-8 generating two fragments, TRAF1(1–163) and TRAF1(164–416), and it is TRAF1(1–163) that is responsible for its inhibitory effects on Trif-mediated signaling.
PMID: 16698941, 16323247
TRAF1 inhibited Trif and TLR3-mediated activation of NF-{kappa}B, IFN-stimulated response element, and IFN-ß promoter activity
indirect
PMID: 16698941, 16415872, 16439361
We identified the Tec kinase, Bruton’s tyrosine kinase (Btk), as the kinase responsible for phosphorylating Mal.
PMID: 16698941
we have shown that after TLR2 and TLR4 stimulation, Mal becomes phosphorylated by Btk and then Mal interacts with SOCS-1, an E3 ligase, mediating Mal polyubiquitination and subsequent degradation via the 26S proteasome.
PMID: 16698941, 12616480, 12721283, 14530355
It has also been reported that MyD88, Trif, and TRAM undergo phosphorylation.
PMID: 16698941, 12616480, 12721283, 14530355
It has also been reported that MyD88, Trif, and TRAM undergo phosphorylation.
PMID: 16698941, 12616480, 12721283, 14530355
It has also been reported that MyD88, Trif, and TRAM undergo phosphorylation.
indirect
PMID: 16698941, 16415872, 16439361
We identified the Tec kinase, Bruton’s tyrosine kinase (Btk), as the kinase responsible for phosphorylating Mal.
PMID: 16698941
we have shown that after TLR2 and TLR4 stimulation, Mal becomes phosphorylated by Btk and then Mal interacts with SOCS-1, an E3 ligase, mediating Mal polyubiquitination and subsequent degradation via the 26S proteasome.
PMID: 16698941
we have shown that after TLR2 and TLR4 stimulation, Mal becomes phosphorylated by Btk and then Mal interacts with SOCS-1, an E3 ligase, mediating Mal polyubiquitination and subsequent degradation via the 26S proteasome.
PMID: 16698941
we have shown that after TLR2 and TLR4 stimulation, Mal becomes phosphorylated by Btk and then Mal interacts with SOCS-1, an E3 ligase, mediating Mal polyubiquitination and subsequent degradation via the 26S proteasome.
PMID: 16698941
we have shown that after TLR2 and TLR4 stimulation, Mal becomes phosphorylated by Btk and then Mal interacts with SOCS-1, an E3 ligase, mediating Mal polyubiquitination and subsequent degradation via the 26S proteasome.
indirect
PMID: 16698941, 15623538
TGF-ß induces MyD88 degradation by the proteasome and so down-regulates TLR signaling.
indirect
PMID: 16698941, 15082713
treatment of the mouse macrophage cell line RAW264.7 with LPS for 1 and 3 h resulted in an increase in IRAK2c mRNA levels, indicating a possible negative-feedback loop.
PMID: 16698941
Unlike IRAK-1, the spliced variant IRAK-1c lacks kinase activity and cannot be phosphorylated by IRAK-4 but still retains its ability to interact with IRAK-2, MyD88, Tollip, and TRAF6.
PMID: 16698941, 12096038
A similar mechanism of decreased IRAK-1 protein was evident following exposure of peritoneal macrophages to the TLR7/8 ligand, R848.
PMID: 16698941, 12096038
A similar mechanism of decreased IRAK-1 protein was evident following exposure of peritoneal macrophages to the TLR7/8 ligand, R848.
PMID: 16698941, 15334086
It has been shown that the de-ubiquitination enzyme A20 terminates TLR signaling by removing ubiquitin moieties from TRAF6.
indirect
PMID: 16698941
it has been shown that ß-arrestins interact with TRAF6 in response to LPS and IL-1ß stimulation
indirect
PMID: 16698941
it has been shown that ß-arrestins interact with TRAF6 in response to LPS and IL-1ß stimulation
PMID: 16698941, 10209148, 12488444, 11588219
ß-Arrestins, in addition to their established roles in receptor desensitization and endocytosis, bind to signaling molecules such as the Src family kinases and the E3 ligase Mdm2.
PMID: 16698941, 10209148, 12488444, 11588219
ß-Arrestins, in addition to their established roles in receptor desensitization and endocytosis, bind to signaling molecules such as the Src family kinases and the E3 ligase Mdm2.
PMID: 16698941, 16378096
In terms of TLR signaling, it has been shown that ß-arrestins negatively regulate TLR signaling by preventing oligomerization of TRAF6, thereby inhibiting its autoubiquitination and subsequent signaling pathways such as NF-{kappa}B and AP-1 activation.
PMID: 16698941
a recent study has shown that the C-domain of TRAF1 interacts with the TIR domain of Trif
PMID: 16698941
it was shown that TRAF1 is cleaved by caspase-8 generating two fragments, TRAF1(1–163) and TRAF1(164–416), and it is TRAF1(1–163) that is responsible for its inhibitory effects on Trif-mediated signaling.
PMID: 16698941, 16323247
Mal and MyD88 interact with TRAF1, suggesting that TRAF1 may negatively regulate Mal and MyD88 signaling, although this remains to be fully explored.
PMID: 16698941, 16323247
Mal and MyD88 interact with TRAF1, suggesting that TRAF1 may negatively regulate Mal and MyD88 signaling, although this remains to be fully explored.
PMID: 16698941, 16306937, 16306936
TRAF3 also interacts directly with Trif and IRAK-1, as well as the IRF3/7 kinases TBK1, IKKi, and putative intracellular viral receptor, protein kinase receptor.
PMID: 16698941, 16306937, 16306936
TRAF3 also interacts directly with Trif and IRAK-1, as well as the IRF3/7 kinases TBK1, IKKi, and putative intracellular viral receptor, protein kinase receptor.
PMID: 16698941, 16306937, 16306936
TRAF3 also interacts directly with Trif and IRAK-1, as well as the IRF3/7 kinases TBK1, IKKi, and putative intracellular viral receptor, protein kinase receptor.
PMID: 16698941, 16306937, 16306936
TRAF3 also interacts directly with Trif and IRAK-1, as well as the IRF3/7 kinases TBK1, IKKi, and putative intracellular viral receptor, protein kinase receptor.
PMID: 16698941, 16306937, 16306936
TRAF3 also interacts directly with Trif and IRAK-1, as well as the IRF3/7 kinases TBK1, IKKi, and putative intracellular viral receptor, protein kinase receptor.
PMID: 16698941, 12692549, 14679297
Activated Trif recruits TBK1 and together with IKKi, mediate IRF3 phosphorylation, dimerization, and nuclear translocation mediating type 1 IFN induction.
PMID: 16698941
we have shown that ST2L, a type I transmembrane protein with three extracellular immunoglobulin-like domains and an intracellular TIR domain, interacts with and sequesters MyD88 and Mal, but not Trif or IRAK
PMID: 16698941
we have shown that ST2L, a type I transmembrane protein with three extracellular immunoglobulin-like domains and an intracellular TIR domain, interacts with and sequesters MyD88 and Mal, but not Trif or IRAK
PMID: 16698941, 16424162
Another molecule, Fliih, has been shown to modulate TLR signaling by interacting with MyD88 and acting as a negative regulator.
PMID: 16698941
overexpression of MyD88s favors formation of MyD88s-MyD88 heterodimers over MyD88 homodimers.
PMID: 16698941
In the presence of these heterodimers, IRAK1 is recruited via the death domain (DD), but it is no longer phosphorylated.