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PMID: 18304834
For example, the TLR2/TLR6 heterodimer can be stimulated by several bacterial components, such as lipoteichoic acid (LTA) and peptidoglycan (PGN)
PMID: 18304834
For example, the TLR2/TLR6 heterodimer can be stimulated by several bacterial components, such as lipoteichoic acid (LTA) and peptidoglycan (PGN)
PMID: 18304834
Viral DNA is rich in unmethylated CpG motifs, which stimulates TLR9
PMID: 1830483
While TLR3 interacts with viral double-stranded RNA, TLR7/8 can sense guanosine- or uridine-rich single-stranded RNA from viruses
PMID: 18304834
While TLR3 interacts with viral double-stranded RNA, TLR7/8 can sense guanosine- or uridine-rich single-stranded RNA from viruses
PMID: 18304834
While TLR3 interacts with viral double-stranded RNA, TLR7/8 can sense guanosine- or uridine-rich single-stranded RNA from viruses
PMID: 1830483,11854525,11062499
Evidence suggests that several PAMPs can stimulate TLR4. These molecules include lipopolysaccharide (LPS) from Gram-negative bacteria, fusion (F) protein from respiratory syncytial virus (RSV) and the envelope protein from mouse mammary tumor virus (MMTV)
PMID: 1830483,11854525,11062499
Evidence suggests that several PAMPs can stimulate TLR4. These molecules include lipopolysaccharide (LPS) from Gram-negative bacteria, fusion (F) protein from respiratory syncytial virus (RSV) and the envelope protein from mouse mammary tumor virus (MMTV)
PMID: 1830483,2427635,2477488
LBP is a soluble shuttle protein which directly binds to LPS and facilitates the association between LPS and CD14
PMID: 1830483,2427635,2477488
LBP is a soluble shuttle protein which directly binds to LPS and facilitates the association between LPS and CD14
PMID: 1830483,1698311
CD14 facilitates the transfer of LPS to the TLR4/MD-2 receptor complex and modulates LPS recognition
PMID: 1830483,1698311
CD14 facilitates the transfer of LPS to the TLR4/MD-2 receptor complex and modulates LPS recognition
PMID: 18304834
By interacting with TLR4/MD-2 directly, RP105/MD-1 can inhibit the association between LPS and TLR4/MD-2.
PMID: 1830483
Upon LPS recognition, TLR4 undergoes oligomerization and recruits its downstream adaptors through interactions with the TIR (Toll-interleukin-1 receptor) domains.
PMID: 1830483,16751103
TIRAP then facilitates the association between MyD88 and the TLR4 cytoplasmic domain to initiate MyD88-dependent downstream signaling
PMID:18304834
ST2L can interact with MyD88 and TIRAP and inhibit their function by sequestration, thereby preventing recruitment to TLR4.
PMID: 1830483,16751103
TIRAP then facilitates the association between MyD88 and the TLR4 cytoplasmic domain to initiate MyD88-dependent downstream signaling
PMID: 1830483,15866876
Another IL-1R homolog, SIGIRR, inhibits TLR4’s interaction with MyD88 through the TIR domain of SIGIRR
PMID:18304834
ST2L can interact with MyD88 and TIRAP and inhibit their function by sequestration, thereby preventing recruitment to TLR4.
PMID: 1830483
. Upon LPS stimulation, MyD88 recruits and activates a death domain-containing kinase, IL-1 receptor-associated kinase-4 (IRAK-4)
PMID: 1830483,15292196
Biochemical evidence also suggests that IRAK-4 is responsible for the subsequent recruitment, activation and degradation of IRAK-1
PMID: 1830483
Another adaptor protein TRAF6 (TNF receptor-associated factor 6), is critical for the MyD88-dependent pathway downstream of IRAK4 and IRAK1
PMID: 1830483,15292196
Biochemical evidence also suggests that IRAK-4 is responsible for the subsequent recruitment, activation and degradation of IRAK-1
PMID: 1830483,
TRAF6 forms a complex with UBC13 (ubiquitin-conjugating enzyme 13) and UEV1A (ubiquitin-conjugating enzyme E2 variant 1 isoform A), and activates TAK1 (transforming growth factor-β-activated kinase 1)
indirect
PMID: 1830483,
TRAF6 forms a complex with UBC13 (ubiquitin-conjugating enzyme 13) and UEV1A (ubiquitin-conjugating enzyme E2 variant 1 isoform A), and activates TAK1 (transforming growth factor-β-activated kinase 1)
PMID: 1830483
TAK1 then activates downstream IKK (IκB kinase) and MAPK (mitogen-activated protein kinase) pathways
PMID: 1830483
IKKalpha, IKKβ and IKKγ form a complex and phosphorylate IκB (inhibitor of κ light chain gene enhancer in B cells) proteins
indirect
PMID: 1830483
TAK1 then activates downstream IKK (IκB kinase) and MAPK (mitogen-activated protein kinase) pathways
indirect
PMID: 1830483
TAK1 then activates downstream IKK (IκB kinase) and MAPK (mitogen-activated protein kinase) pathways
indirect
PMID: 18304834
This phosphorylation leads to the degradation of IκB proteins and the subsequent translocation of the transcription factor NF-κB, which controls the expression of proinflammatory cytokines, in addition to other immune related genes.
PMID: 18304834
TRIF induces the cleavage of TRAF1 by caspases (likely caspase-8) and the cleaved fragment of TRAF1 can inhibit TRIF-induced NF-κB and IRF3 activation
PMID: 1830483
This phosphorylation leads to the degradation of IκB proteins and the subsequent translocation of the transcription factor NF-κB, which controls the expression of proinflammatory cytokines, in addition to other immune related genes.
PMID: 1830483
This phosphorylation leads to the degradation of IκB proteins and the subsequent translocation of the transcription factor NF-κB, which controls the expression of proinflammatory cytokines, in addition to other immune related genes.
indirect
PMID: 1830483
This phosphorylation leads to the degradation of IκB proteins and the subsequent translocation of the transcription factor NF-κB, which controls the expression of proinflammatory cytokines, in addition to other immune related genes.
indirect
PMID: 1830483
Activation of the downstream MAPK pathways leads to the induction of another transcription factor AP-1
indirect
PMID: 1830483
Activation of the downstream MAPK pathways leads to the induction of another transcription factor AP-1,which also has a role in the expression of proinflammatory cytokines
PMID: 1830483
TRIF is an important TIR-containing adaptor protein that mediates MyD88-independent signaling
PMID: 1830483
TRIF is an important TIR-containing adaptor protein that mediates MyD88-independent signaling
PMID: 18304834
The C-terminal region of TRIF, which contains a Rip homotypic interaction motif (RHIM), mediates the interaction with RIP1 (receptor-interacting protein 1).
PMID: 1830483
Experiments suggest that TRIF recruits TRAF3 to activate IRF3, and accordingly the induction of Type I interferons was defective in TRAF3-deficient cells
PMID: 18304834,16306936,17327220
TRAF3 can associate with TANK (TRAF family member-associated NF-κB activator), TBK1 (TANK binding kinase 1) and IKKi to mediate downstream signaling
indirect
PMID: 18304834,12692549,15210742
Experiments suggest that TRIF recruits TRAF3 to activate IRF3, and accordingly the induction of Type I interferons was defective in TRAF3-deficient cells
PMID: 18304834
TRIF induces the cleavage of TRAF1 by caspases (likely caspase-8) and the cleaved fragment of TRAF1 can inhibit TRIF-induced NF-κB and IRF3 activation
PMID: 18304834,12692549,15210742
TBK1 and IKKi are important for the dimerization and translocation of IRF3
PMID: 18304834,12692549,15210742
TBK1 and IKKi are important for the dimerization and translocation of IRF3
indirect
PMID: 18304834,16006187,16932750
IRF3, together with NF-κB, activates the transcription of target genes, such as Type I interferons
indirect
PMID: 18304834
TRIF signals the induction of
Type I interferons by recruiting TRAF3 and RIP1 to activate transcription
factor IRF3, as well as NF-KappaB and AP-1.
indirect
PMID: 18304834
TRIF signals the induction of
Type I interferons by recruiting TRAF3 and RIP1 to activate transcription
factor IRF3, as well as NF-KappaB and AP-1.
PMID: 18304834
Originally identified in B cells, RP105 is a homolog of TLR4 and associates with the MD-2 homolog MD-1.
PMID: 18304834
By interacting with TLR4/MD-2 directly, RP105/MD-1 can inhibit the association between LPS and TLR4/MD-2
PMID:18304834
ST2 L can interact with MyD88 and TIRAP and inhibit their function by sequestration, thereby preventing recruitment to TLR4.
PMID:18304834
ST2L can interact with MyD88 and TIRAP and inhibit their function by sequestration, thereby preventing recruitment to TLR4.
PMID: 18304834,16968706
TRIAD3A can interact with certain TIR domain containing proteins, such as TIRAP, TRIF and RIP1
PMID: 18304834,16968706
TRIAD3A can interact with certain TIR domain containing proteins, such as TIRAP, TRIF and RIP1
PMID: 18304834,16968706
TRIAD3A can interact with certain TIR domain containing proteins, such as TIRAP, TRIF and RIP1
indirect
PMID: 18304834,15866876,15107846
Overexpression of TRIAD3A can promote the degradation of TLR4, TIRAP, TRIF and RIP1 [
indirect
PMID: 18304834,15866876,15107846
Overexpression of TRIAD3A can promote the degradation of TLR4, TIRAP, TRIF and RIP1 [
PMID: 18304834,15866876,15107846
Overexpression of TRIAD3A can promote the degradation of TLR4, TIRAP, TRIF and RIP1 [
indirect
PMID: 18304834,15866876,15107846
Overexpression of TRIAD3A can promote the degradation of TLR4, TIRAP, TRIF and RIP1 [
PMID: 18304834,15107846
TRIAD3A overexpression can downregulate NF-κB activation, and knockingdown TRIAD3A expression upregulates NF-κB activation upon LPS stimulation
PMID: 18304834,16415872
TRAF4 overexpression can inhibit NF-κB activation possibly through the interaction with TRIF and TRAF6
indirect
PMID: 18304834
SOCS-1 can induce the ubiquitination of TIRAP which leads to its subsequent degradation
PMID: 18304834
SOCS-1 can induce the ubiquitination of TIRAP which leads to its subsequent degradation
PMID: 1830483,15292196
Biochemical evidence also suggests that IRAK-4 is responsible for the subsequent recruitment, activation and degradation of IRAK-1
PMID: 18304834
Studies have suggested that IRAK-M inhibits MyD88-mediated signaling by preventing the dissociation of IRAKs from MyD88.
indirect
indirect
PMID: 18304834
TRIF induces the cleavage of TRAF1 by caspases (likely caspase-8) and the cleaved fragment of TRAF1 can inhibit TRIF-induced NF-κB and IRF3 activation
PMID: 18304834,16415872
TRAF4 overexpression can inhibit NF-κB activation possibly through the interaction with TRIF and TRAF6
PMID: 18304834,16415872
TRAF4 overexpression can inhibit NF-κB activation possibly through the interaction with TRIF and TRAF6
PMID: 18304834
For example, the TLR2/TLR6 heterodimer can be stimulated by several bacterial components, such as lipoteichoic acid (LTA) and peptidoglycan (PGN)