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PMID: 17449723
Upon activation, TLRs interact intracellularly with these adaptor proteins via TIR domains, and the adaptor proteins then recruit and activate downstream molecules such as IL-1R-associated kinases (IRAKs) and TNF-receptor-associated factor-6 (TRAF6), which then amplify the signal.
PMID: 17449723
In cases of infection, LPS, derived from gram-negative bacteria, binds TLR4 dimers.
PMID: 17449723
i) Mal is synthesized and produced and ii) binds PIP2 in the plasma membrane via its PIP2-binding domain.
PMID: 17449723, 10589680
It was also shown that the localization of Mal to the plasma membrane by PIP2 binding is dependent on the β2-integrin CD11b in macrophages and also on the GTPase ADP ribosylation factor 6 (ARF6), which regulates production of PIP2 via activation of the enzyme PI-5K.
PMID: 17449723
Upon activation, TLRs interact intracellularly with these adaptor proteins via TIR domains, and the adaptor proteins then recruit and activate downstream molecules such as IL-1R-associated kinases (IRAKs) and TNF-receptor-associated factor-6 (TRAF6), which then amplify the signal.
PMID: 17449723
Upon activation, TLRs interact intracellularly with these adaptor proteins via TIR domains, and the adaptor proteins then recruit and activate downstream molecules such as IL-1R-associated kinases (IRAKs) and TNF-receptor-associated factor-6 (TRAF6), which then amplify the signal.
PMID: 17449723
Upon activation, TLRs interact intracellularly with these adaptor proteins via TIR domains, and the adaptor proteins then recruit and activate downstream molecules such as IL-1R-associated kinases (IRAKs) and TNF-receptor-associated factor-6 (TRAF6), which then amplify the signal.
PMID: 17449723, 16698941
TLR signaling ultimately results in the activation of transcription factors such as NF-{kappa}B and IFN regulatory factors (IRFs), which promote the transcription of proinflammatory cytokines and other proteins that promote host defense.
PMID: 17449723, 16698941
TLR signaling ultimately results in the activation of transcription factors such as NF-{kappa}B and IFN regulatory factors (IRFs), which promote the transcription of proinflammatory cytokines and other proteins that promote host defense.
PMID: 17449723, 16698941
TLR signaling ultimately results in the activation of transcription factors such as NF-{kappa}B and IFN regulatory factors (IRFs), which promote the transcription of proinflammatory cytokines and other proteins that promote host defense.
PMID: 17449723
It colocalizes with TLR4.
PMID: 17449723, 10589680
It was also shown that the localization of Mal to the plasma membrane by PIP2 binding is dependent on the β2-integrin CD11b in macrophages and also on the GTPase ADP ribosylation factor 6 (ARF6), which regulates production of PIP2 via activation of the enzyme PI-5K.
PMID: 17449723, 16751103
his protein has been shown to interrupt Mal localization and therefore, disrupt TLR4 signaling.
PMID: 17449723
This leads to MyD88 recruitment to the Mal/TLR4 complex. MyD88 can then interact with downstream signaling molecules such as IRAK-4 and IRAK-1.
PMID: 17449723
This leads to MyD88 recruitment to the Mal/TLR4 complex. MyD88 can then interact with downstream signaling molecules such as IRAK-4 and IRAK-1.
PMID: 17449723
It was shown that Mal can bind TRAF6 directly and that mutating this TRAF6-binding site creates a dominant-negative mutant of NF-{kappa}B activation and activation of MAPKs by TLR2 and TLR4.
PMID: 17449723
MyD88 does, however, bind IRAK-1, which contains a TRAF6-binding site, leading to NF-{kappa}B activation.
PMID: 17449723
By an as-yet-unknown mechanism, Btk is activated following LPS stimulation of the cell.
PMID: 17449723
Mal recruits MyD88 to TLR2 and TLR4, and TRAM recruits TRIF to TLR4.
PMID: 17449723, 16439361
Gray et al. [27 ] demonstrated that Mal can be tyrosine-phosphorylated at residues 86 and 187 by Bruton’s tyrosine kinase (Btk) following activation of TLR2 and TLR4.
Indirect
PMID: 17449723, 16439361
Gray et al. [27 ] demonstrated that Mal can be tyrosine-phosphorylated at residues 86 and 187 by Bruton’s tyrosine kinase (Btk) following activation of TLR2 and TLR4.
PMID: 17449723
SOCS-1 recognizes a proline, glutamic acid, serine, and threonine-rich area domain (PEST) in Mal, N-terminal to its TIR domain and subsequently, targets Mal for degradation by the addition of ubiquitin to lysine side-chains at amino acid positions 15 and 16.
PMID: 17449723
Phospho-Mal is recognized by the ubiquitin ligase SOCS-1 (whose expression also increases in response to LPS).
PMID: 17449723
Phospho-Mal is recognized by the ubiquitin ligase SOCS-1 (whose expression also increases in response to LPS).
PMID: 17449723
SOCS-1 uses its E3 ligase activity to attach ubiquitin residues to Mal.
PMID: 17449723
This ubiquitination step targets Mal for degradation by the 26S proteasome.Mal is removed from the membrane. MyD88 can no longer interact directly with TLR4 and also leaves the membrane.
PMID: 17449723
Mal recruits MyD88 to TLR2 and TLR4, and TRAM recruits TRIF to TLR4.
PMID: 17449723
Mal recruits MyD88 to TLR2 and TLR4, and TRAM recruits TRIF to TLR4.
PMID: 17449723
Mal recruits MyD88 to TLR2 and TLR4, and TRAM recruits TRIF to TLR4.
PMID: 17449723
TRAM is myristoylated in its N-terminus and becomes attached to the membrane in association with TLR4.
PMID: 17449723
Mal recruits MyD88 to TLR2 and TLR4, and TRAM recruits TRIF to TLR4.
PMID: 17449723
This leads to the recruitment of TRIF to the TRAM/TLR4 complex.
PMID: 17449723
It was also shown that treatment of cells with LPS enhances SARM expression, and it has been speculated that following TLR4 activation, SARM levels increase in cells and eventually bind TRIF to limit the LPS-driven response.
PMID: 17449723
The MyD88 pathway leads to activation of the transcription factors NF-{kappa}B, IRF1, IRF5, and IRF7.
PMID: 17449723
The MyD88 pathway leads to activation of the transcription factors NF-{kappa}B, IRF1, IRF5, and IRF7.
PMID: 17449723
The MyD88 pathway leads to activation of the transcription factors NF-{kappa}B, IRF1, IRF5, and IRF7.
PMID: 17449723
The MyD88 pathway leads to activation of the transcription factors NF-{kappa}B, IRF1, IRF5, and IRF7.
PMID: 17449723
The MyD88 pathway leads to activation of the transcription factors NF-{kappa}B, IRF1, IRF5, and IRF7.
PMID: 17449723
The MyD88 pathway leads to activation of the transcription factors NF-{kappa}B, IRF1, IRF5, and IRF7.
PMID: 17449723, 12609980
Following the discovery that activation of NF-{kappa}B, p38 MAPK, and JNK was impaired in MyD88-deficient cells in response to all TLRs, except in the case of TLR3.
PMID: 17449723, 12609980
Following the discovery that activation of NF-{kappa}B, p38 MAPK, and JNK was impaired in MyD88-deficient cells in response to all TLRs, except in the case of TLR3.
PMID: 17449723, 12609980
Following the discovery that activation of NF-{kappa}B, p38 MAPK, and JNK was impaired in MyD88-deficient cells in response to all TLRs, except in the case of TLR3.
PMID: 17449723, 16166516
The effect of TRIF here is to induce TNF-{alpha} production via activation of IRF3, with TNF-{alpha} acting in an autocrine manner to induce the late activation of NF-{kappa}B.
PMID: 17449723, 16166516
The effect of TRIF here is to induce TNF-{alpha} production via activation of IRF3, with TNF-{alpha} acting in an autocrine manner to induce the late activation of NF-{kappa}B.
PMID: 17449723
TRAM is myristoylated in its N-terminus and becomes attached to the membrane in association with TLR4.
PMID: 17449723
TRIF then interacts with downstream signaling molecules such as Tank-binding kinase-1, which phosphorylates and activates the transcription factor IRF3.
PMID: 17449723
TRIF then interacts with downstream signaling molecules such as Tank-binding kinase-1, which phosphorylates and activates the transcription factor IRF3.
PMID: 17449723
TRIF also interacts with TRAF6 and receptor-interacting protein-1, which brings about the activation of NF-{kappa}B.
PMID: 17449723
By an as-yet-unknown mechanism, PKC{epsilon} is activated in response to LPS.
PMID: 17449723, 11696589, 9601053
The kinase responsible for phosphorylation of TRAM was found to be protein kinase C {epsilon} (PKC{epsilon}), which was known to have a role in LPS signaling [36 ], and its activation by other signaling molecules such as diacyglycerol [37 ] may again provide another level of control in the LPS response.
PMID: 17449723
PKC{epsilon} phosphorylates TRAM at serine 16.
PMID: 17449723
PKC{epsilon} phosphorylates TRAM at serine 16.
PMID: 17449723
This phosphorylation event may also cause TRAM to leave the membrane. viii) With TRAM depleted from the membrane, TRIF no longer interacts with TLR4 and also leaves the membrane. This disrupts the signaling pathway and limits the response to LPS.
PMID: 17449723
TLR4 is also degraded at this point.
PMID: 17449723
This phosphorylation event may also cause TRAM to leave the membrane. viii) With TRAM depleted from the membrane, TRIF no longer interacts with TLR4 and also leaves the membrane. This disrupts the signaling pathway and limits the response to LPS.
PMID: 17449723
TLR4 is also degraded at this point.
PMID: 17449723
ARF6 is activated by integrins.
PMID: 17449723, 10589680
It was also shown that the localization of Mal to the plasma membrane by PIP2 binding is dependent on the β2-integrin CD11b in macrophages and also on the GTPase ADP ribosylation factor 6 (ARF6), which regulates production of PIP2 via activation of the enzyme PI-5K.
PMID: 17449723
The MyD88 pathway leads to activation of the transcription factors NF-{kappa}B, IRF1, IRF5, and IRF7.
PMID: 17449723
MyD88 does, however, bind IRAK-1, which contains a TRAF6-binding site, leading to NF-{kappa}B activation.
PMID: 17449723
This phosphorylation is required for the activation of a pathway culminating in transactivation by the NF-{kappa}B subunit p65 via phosphorylation on serine 536.
PMID: 17449723
TRIF also interacts with TRAF6 and receptor-interacting protein-1, which brings about the activation of NF-{kappa}B.
PMID: 17449723, 16698941
TLR signaling ultimately results in the activation of transcription factors such as NF-{kappa}B and IFN regulatory factors (IRFs), which promote the transcription of proinflammatory cytokines and other proteins that promote host defense.
PMID: 17449723, 16166516
The effect of TRIF here is to induce TNF-{alpha} production via activation of IRF3, with TNF-{alpha} acting in an autocrine manner to induce the late activation of NF-{kappa}B.
PMID: 17449723, 16807108
These proteins, similar to TLRs, respond to PAMPs, usually in the cytoplasmic environment.
PMID: 17449723
Caspase-1 must be activated in inflammasomes, which consist of another group of an innate pathogen sensor, nucleotide oligomerization domain-like receptors (NLRs), including the proteins Nalp1, Nalp3, and Ipaf.
PMID: 17449723, 17360653
Another interesting feature of Mal is its recently discovered ability to interact with caspase-1 [32 ], which is an important inflammatory caspase, responsible for cleavage of pro-IL-1beta into a catalytically active form secreted by cells.
PMID: 17449723, 17360653
Another interesting feature of Mal is its recently discovered ability to interact with caspase-1 [32 ], which is an important inflammatory caspase, responsible for cleavage of pro-IL-1beta into a catalytically active form secreted by cells.
PMID: 17449723
The SARM protein interacts with TRIF, and this interaction requires its TIR domain.
PMID: 17449723
This interaction is weak in untreated cells but is enhanced by LPS or dsRNA treatment.
PMID: 17449723
The SARM protein interacts with TRIF, and this interaction requires its TIR domain.
PMID: 17449723
This interaction is weak in untreated cells but is enhanced by LPS or dsRNA treatment.
PMID: 17449723
It was also shown that treatment of cells with LPS enhances SARM expression, and it has been speculated that following TLR4 activation, SARM levels increase in cells and eventually bind TRIF to limit the LPS-driven response.
PMID: 17449723, 10589680
It was also shown that the localization of Mal to the plasma membrane by PIP2 binding is dependent on the β2-integrin CD11b in macrophages and also on the GTPase ADP ribosylation factor 6 (ARF6), which regulates production of PIP2 via activation of the enzyme PI-5K.