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indirect
PMID: 17395581, 16497588
This binding leads to the activation of IFN-stimulated gene factor 3 (ISGF3; a heterotrimer of signal transducer and activator of transcription 1 (STAT1), STAT2, and IFN regulatory factor 9 (IRF9)), which translocates to the nucleus and induces the transcription of hundreds of effector molecules, called IFN-inducible genes.
PMID: 17395581, 16497588
This binding leads to the activation of IFN-stimulated gene factor 3 (ISGF3; a heterotrimer of signal transducer and activator of transcription 1 (STAT1), STAT2, and IFN regulatory factor 9 (IRF9)), which translocates to the nucleus and induces the transcription of hundreds of effector molecules, called IFN-inducible genes.
PMID: 17395581, 16497588
This binding leads to the activation of IFN-stimulated gene factor 3 (ISGF3; a heterotrimer of signal transducer and activator of transcription 1 (STAT1), STAT2, and IFN regulatory factor 9 (IRF9)), which translocates to the nucleus and induces the transcription of hundreds of effector molecules, called IFN-inducible genes.
PMID: 17395581
These effector molecules directly influence protein synthesis, cell growth, and survival, in the process of establishing an antiviral state.
PMID: 17395581, 9851930, 10201887
TLR4, the first mammalian homologue of the Drosophila Toll protein recognizes lipopolysaccharide (LPS), which is a cell wall component of Gram-negative bacteria
PMID: 17395581, 11062499, 11854525
TLR4 recognizes not only bacterial components but also viral proteins, such as the fusion (F) protein from respiratory syncytial virus and the envelope protein of mouse mammary tumor virus.
PMID: 17395581, 11062499, 11854525
TLR4 recognizes not only bacterial components but also viral proteins, such as the fusion (F) protein from respiratory syncytial virus and the envelope protein of mouse mammary tumor virus.
PMID: 17395581, 16497588
Each TLR mediates distinctive responses in association with a different combination of four TIR domain-containing adapters (MyD88, TIRAP/MAL, TRIF, and TRAM) through the homophilic interaction of TIR domains.
PMID: 17395581
A TIR domain-containing adapter, MyD88, associates with the cytoplasmic TIR domain of TLRs and recruits IRAKs to the receptor upon ligand binding.
PMID: 17395581
The association of TLRs with MyD88, which is utilized by all TLRs except TLR3, recruits IL-1R-associated kinase (IRAK)-1 and IRAK-4 and tumor necrosis factor receptor-associated factor 6 (TRAF6).
PMID: 17395581
The association of TLRs with MyD88, which is utilized by all TLRs except TLR3, recruits IL-1R-associated kinase (IRAK)-1 and IRAK-4 and tumor necrosis factor receptor-associated factor 6 (TRAF6).
PMID: 17395581
The association of TLRs with MyD88, which is utilized by all TLRs except TLR3, recruits IL-1R-associated kinase (IRAK)-1 and IRAK-4 and tumor necrosis factor receptor-associated factor 6 (TRAF6).
PMID: 17395581
IRAKs then activate TRAF6, leading to the activation of TAK1.
PMID: 17395581
IRAK-1 and TRAF6 then dissociate from this receptor complex and associate with another complex composed of transforming growth factor-beta-activated kinase (TAK1) and TAK1-binding proteins 1 (Tab1) and 2.
PMID: 17395581
IRAK-1 and TRAF6 then dissociate from this receptor complex and associate with another complex composed of transforming growth factor-beta-activated kinase (TAK1) and TAK1-binding proteins 1 (Tab1) and 2.
PMID: 17395581
This complex formation leads to the activation of TAK1.
indirect
PMID: 17395581
TAK1 activates the IKK complex consisting of IKK{alpha}, IKKbeta, and NEMO/IKK{gamma}.
PMID: 17395581
The IKK complex phosphorylates I{kappa}B, resulting in nuclear translocation of NF-{kappa}B, which induces expression of inflammatory cytokines.
PMID: 17395581
The IKK complex phosphorylates I{kappa}B, resulting in nuclear translocation of NF-{kappa}B, which induces expression of inflammatory cytokines.
PMID: 17395581
The IKK complex phosphorylates I{kappa}B, resulting in nuclear translocation of NF-{kappa}B, which induces expression of inflammatory cytokines.
indirect
PMID: 17395581
This complex formation leads to the activation of TAK1, which in turn activates the transcription factors nuclear factor-{kappa}B (NF-{kappa}B) and activator protein 1 (AP-1) through the canonical I{kappa}B kinase (IKK) complex and the mitogen-activated protein kinase pathway, respectively.
indirect
PMID: 17395581
This complex formation leads to the activation of TAK1, which in turn activates the transcription factors nuclear factor-{kappa}B (NF-{kappa}B) and activator protein 1 (AP-1) through the canonical I{kappa}B kinase (IKK) complex and the mitogen-activated protein kinase pathway, respectively.
PMID: 17395581
TLR4 also requires another adapter, TRAM, for IRF3 activation.
PMID: 17395581
The N terminus of TRAM has a myristoylation site, mutation of which alters its normal membrane localization and abolishes TLR4 signaling, suggesting that TRAM acts as a bridging adapter between TLR4 and TRIF
PMID: 17395581
TLR4 also requires another adapter, TRAM, for IRF3 activation.A TIR domain-containing adapter, TRIF, is responsible for TLR3- and TLR4-mediated IRF3 activation
PMID: 17395581, 16757566
It has also been reported that phosphorylation of TRAM by PKC{epsilon} is crucial for the activation of IRF3 and the induction of IFN-inducible genes.
PMID: 17395581, 15064760
Receptor-interacting protein-1 (RIP1) binds the C terminus of TRIF via a Rip homotypic interaction motif and mediates the TLR3-mediated NF-{kappa}B but not IRF3 activation.
PMID: 17395581
TRAF6 binds the N terminus of TRIF and cooperatively activates NF-kappaB.
PMID: 17395581
TRIF interacts with TBK1, IKK{iota}, RIP1, and TRAF6.
PMID: 17395581
IRF3 is activated by TBK1 and IKK{iota}, which catalyze IRF3 phosphorylation and stimulate its nuclear translocation and DNA binding.
PMID: 17395581
IRF3 is activated by TBK1 and IKK{iota}, which catalyze IRF3 phosphorylation and stimulate its nuclear translocation and DNA binding.
PMID: 17395581
IRF3 is activated by TBK1 and IKK{iota}, which catalyze IRF3 phosphorylation and stimulate its nuclear translocation and DNA binding.
PMID: 17395581, 16473828, 16858407
TLR3 interacts with CD14 and c-Src for ligand uptake and signal transduction.
PMID: 17395581, 16497588
TLR3 recognizes a synthetic analog of viral dsRNA, polyinosinic acid-cytidylic acid (poly(I·C)), and viral dsRNAs derived from dsRNA viruses such as reovirus or ssRNA viruses such as West Nile virus, respiratory syncytial virus, and encephalomyocarditis virus.
PMID: 17395581, 12872135, 12855817
TLR3 signaling activates the transcription factors interferon regulatory factor 3 (IRF3) and NF-{kappa}B via the adapter molecule TRIF.
PMID: 17395581, 15064760
Receptor-interacting protein-1 (RIP1) binds the C terminus of TRIF via a Rip homotypic interaction motif and mediates the TLR3-mediated NF-{kappa}B but not IRF3 activation.
PMID: 17395581, 16306936, 16306937, 15611223, 12702806
TRIF interacts with noncanonical IKKs TBK1 (also called NAK or T2K) and IKK{iota} (also called IKK{epsilon}) through TRAF3 and NAK-associated protein 1 (NAP1), which mediate phosphorylation of IRF3.
indirect
PMID: 17395581, 16306936, 16306937, 15611223, 12702806
TRIF interacts with noncanonical IKKs TBK1 (also called NAK or T2K) and IKK{iota} (also called IKK{epsilon}) through TRAF3 and NAK-associated protein 1 (NAP1), which mediate phosphorylation of IRF3.
PMID: 17395581, 16699525
IRF3 activation is negatively regulated by the peptidyl-prolyl isomerase Pin1.
PMID: 17395581
Activated IRF3 translocates into the nucleus and induces expression of IFN-beta.
PMID: 17395581, 16323247, 16052631
TRAF1 and TRAF4 interact with TRIF and negatively regulate TRIF-mediated signaling pathways.
PMID: 17395581, 14530355
TRAF6 binds the N terminus of TRIF and cooperatively activates NF-{kappa}B.
indirect
PMID: 17395581, 14530355
TRAF6 binds the N terminus of TRIF and cooperatively activates NF-{kappa}B.
PMID: 17395581, 11130078
TLR9 mediates the recognition of CpG DNA.
indirect
PMID: 17395581, 12900525
Mouse pDCs produce IFN-{alpha} by recognizing the CpG-containing DNA of herpes simplex virus type 2 (HSV-2) via TLR9.
indirect
PMID: 17395581, 14976261, 14976262
TLR7 and human TLR8 have been shown to recognize guanosine- or uridine-rich ssRNA from viruses such as human immunodeficiency virus, vesicular stomatitis virus, and influenza virus
PMID: 17395581, 14976261, 14976262
TLR7 and human TLR8 have been shown to recognize guanosine- or uridine-rich ssRNA from viruses such as human immunodeficiency virus, vesicular stomatitis virus, and influenza virus.
PMID: 17395581, 12626561
The induction of type I IFNs by TLR7 and TLR9 depends entirely on MyD88 in pDCs.
PMID: 17395581, 12626561
The induction of type I IFNs by TLR7 and TLR9 depends entirely on MyD88 in pDCs.
indirect
PMID: 17395581, 12626561
The induction of type I IFNs by TLR7 and TLR9 depends entirely on MyD88 in pDCs.
indirect
PMID: 17395581, 12626561
The induction of type I IFNs by TLR7 and TLR9 depends entirely on MyD88 in pDCs.
PMID: 17395581
IRF7 is activated through forming a signaling complex with MyD88, IRAKs, and TRAF6 in the cytoplasm.
PMID: 17395581, 15361868, 15492225
IRF7 forms a signaling complex with MyD88 and TRAF6 in the cytoplasm.
PMID: 17395581, 15361868, 15492225, 17056502
After ligand stimulation, IRF7 is activated by its phosphorylation in TBK1/IKK{iota}-independent manner and translocates into the nucleus to induce the expression of type I IFNs.
PMID: 17395581, 15767370
IRAK-1, but not IRAK-4, can directly bind and phosphorylate IRF7; thus, IRAK-1 specifically mediates IFN-{alpha} induction downstream of MyD88 and IRAK-4
PMID: 17395581, 15361868, 15492225, 17056502
After ligand stimulation, IRF7 is activated by its phosphorylation in TBK1/IKK{iota}-independent manner and translocates into the nucleus to induce the expression of type I IFNs.
PMID: 17395581, 16612387
In addition to IRAKs, IKK{alpha} has been shown to be essential for the phosphorylation of IRF7, suggesting that the IRAK-4/IRAK-1/IKK{alpha} kinase cascade might lead to the full activation of IRF7.
PMID: 17395581, 17018642
After ligand stimulation, IRF1 interacts with MyD88, is activated by an unknown mechanism, and translocates into the nucleus to induce the expression of IFN-beta, inducible nitric-oxide synthase, and IL-12 p35.
PMID: 17395581, 17018642
After ligand stimulation, IRF1 interacts with MyD88, is activated by an unknown mechanism, and translocates into the nucleus to induce the expression of IFN-beta, inducible nitric-oxide synthase, and IL-12 p35.
MID: 17395581, 17018642
After ligand stimulation, IRF1 interacts with MyD88, is activated by an unknown mechanism, and translocates into the nucleus to induce the expression of IFN-beta, inducible nitric-oxide synthase, and IL-12 p35.
MID: 17395581, 17018642
After ligand stimulation, IRF1 interacts with MyD88, is activated by an unknown mechanism, and translocates into the nucleus to induce the expression of IFN-beta, inducible nitric-oxide synthase, and IL-12 p35.
MID: 17395581, 17018642
After ligand stimulation, IRF1 interacts with MyD88, is activated by an unknown mechanism, and translocates into the nucleus to induce the expression of IFN-beta, inducible nitric-oxide synthase, and IL-12 p35.
PMID: 17395581
Type I IFNs are the key cytokines that mediate antiviral responses. Secreted IFNs bind and activate the type I IFN receptor (a heterodimer of IFNAR1 and IFNAR2) in an autocrine and paracrine manner.