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PMID: 16357866, 2402637 LBP is an acute-phase protein, the role of which is to bring LPS to the cell surface by binding to LPS and forming a ternary complex with the LPS receptor molecule, CD14. PMID: 16357866, 11274165 Formation of the complex between LPS and CD14 facilitates the transfer of LPS to the LPS receptor complex composed of TLR4 and MD2. PMID: 16357866, 15852007 The complex of RP105 and MD1 interacts with TLR4/MD2, impairing its ability to bind LPS. PMID: 16357866, 12072369, 11276205 LPS associates with the heat shock proteins, Hsp70 and Hsp90, chemokine receptor 4 (CXCR4) and growth differentiation factor 5 (GDF5). PMID: 16357866, 12691620 MyD88 is recruited to the TLR4 receptor through interaction with the TIR domain of TLR4. PMID: 16357866, 11544529 Upon LPS stimulation, TIRAP also associates with TLR4 via a TIR–TIR interaction, and is essential for MyD88-dependent signaling. PMID: 16357866, 15004556 The inhibitory effect of ST2 is the result of the interaction between its TIR domain and the TIR domains of MyD88 and TIRAP, thus sequestering these critical adaptors during LPS signaling. PMID: 16357866 IRAK-M plays a negative role in TLR4 signaling by preventing the dissociation of IRAK4 and MyD88 and thus preventing the formation of the IRAK–TRAF6 complex. PMID: 16357866, 14519765 MyD88-independent signaling begins with recruitment of the adaptor molecule, TRAM, to the cytoplasmic domain of TLR4. PMID: 16357866, 14519765, 14556004 TRAM is specific to the TLR4 signaling pathway and was cloned as a TLR4-binding protein in yeast that facilitates the binding of TRIF to the receptor complex by forming heterodimers with TRIF. PMID: 16357866, 12538665 The binding of IRAK4 to the receptor complex facilitates the transphosphorylation of IRAK1, inducing IRAK1 kinase activity. PMID: 16357866, 12538665 MyD88s inhibits TLR4 signaling by preventing the recruitment of IRAK4 to MyD88 in the receptor complex, thus abolishing phosphorylation and activation of IRAK1. PMID: 16357866, 8837778 The autophosphorylation and activation of IRAK1 results in the ability to bind TNF receptor-associated factor-6 (TRAF6). PMID: 16357866 The complex of IRAK1 and TRAF6 dissociates from the receptor. PMID: 16357866 IRAK-M plays a negative role in TLR4 signaling by preventing the dissociation of IRAK4 and MyD88 and thus preventing the formation of the IRAK–TRAF6 complex. PMID: 16357866, 12242293 The complex of IRAK1 and TRAF6 dissociates from the receptor to form a complex at the membrane with transforming growth factor-b (TGFb)-activated kinase 1 (TAK1) and the adaptor molecules, TAK1-binding protein 1 and 2 (TAB1 and TAB2). a third adaptor molecule has been identified, TAB3, which also interacts with TAK1. PMID: 16357866, 10882101, 15836773 TAB2 links TAK1 to TRAF6 and facilitates the ubiquitination of TRAF6. PMID: 16357866 it forms a complex with the ubiquitin conjugating enzyme Ubc13 and the Ubc-like protei. PMID: 16357866 When TAK1 is activated, IRAK1 is released from the complex. PMID: 16357866, 9261174 When TAK1 is activated, IRAK1 is released from the complex and eventually degraded by the ubiquitin–proteasome system. Indirect PMID: 16357866, 14550571 TRAF6 is recycled through the process of deubiquitination. PMID: 16357866 A20 is dependent on its ability to act as a TRAF6 deubiquitinase. Indirect PMID: 16357866, 11460167 TAK1-mediated phosphorylation of the IkB kinase (IKK) complex, composed of two catalytic subunits, IKKa and IKKb, and a regulatory subunit, IKK-gamma, also known as NF-kappaB essential modulator (NEMO). Indirect PMID: 16357866 Activation of the IKKs leads to downstream phosphorylation of members of the inhibitor of NF-kappaB (IkB) family. PMID: 16357866, 7628694 Activation of the IKKs leads to downstream phosphorylation of members of the inhibitor of NF-kappaB (IkappaB) family, resulting in ubiquitin-directed proteasome- mediated degradation of the IkappaB members, thus permitting the release and nuclear translocation of the transcription factor, NF-kappaB. Indirect PMID: 16357866, 11460167 activation of TAK1 also leads to activation of a family of MAPKs consisting of p38, extracellular signal-regulated kinase (ERK) and c-jun NH2-terminal kinase (JNK). PMID: 16357866 SHIP1 also inhibits LPS-induced MAPK activation and IkB-a degradation. Indirect PMID: 16357866, 11460167 activation of TAK1 also leads to activation of a family of MAPKs consisting of p38, extracellular signal-regulated kinase (ERK) and c-jun NH2-terminal kinase (JNK). PMID: 16357866, 15699069 Overexpression of Dok1 or Dok2 inhibits LPS-induced ERK activation. PMID: 16357866 SHIP1 also inhibits LPS-induced MAPK activation and IkB-a degradation. Indirect Indirect Indirect PMID: 16357866, 11460167 activation of TAK1 also leads to activation of a family of MAPKs consisting of p38, extracellular signal-regulated kinase (ERK) and c-jun NH2-terminal kinase (JNK). PMID: 16357866, 14699155 LPS-induced JNK activation involves the participation of the protein tyrosine kinase, Syk, and PI3K. PMID: 16357866 SHIP1 also inhibits LPS-induced MAPK activation and IkB-a degradation. Indirect PMID: 16357866, 12193732 MEKK3 activates both NF-kB and p38 kinase, but not ERK, by binding to TRAF6 in mouse embryonic fibroblasts (MEFs). PMID: 16357866 SHIP1 also inhibits LPS-induced MAPK activation and IkB-a degradation. PMID: 16357866, 12193732 MEKK3 activates both NF-kB and p38 kinase, but not ERK, by binding to TRAF6 in mouse embryonic fibroblasts (MEFs). Indirect PMID: 16357866, 12193732 MEKK3 activates both NF-kB and p38 kinase, but not ERK, by binding to TRAF6 in mouse embryonic fibroblasts (MEFs). PMID: 16357866, 12659860 Expression of A20 inhibits TLR4-mediated NF-kappaB activation by regulating MEKK-1 kinase activity. PMID: 16357866, 12433373, 12433365 ectopic expression of SOCS1 in a macrophage cell line inhibits LPSinduced NF-kappaB activation. PMID: 16357866 A1 inhibits endothelial activation by inhibiting NF-kB activity. PMID: 16357866 Activation of the IKKs leads to downstream phosphorylation of members of the inhibitor of NF-kappaB (IkappaB) family, resulting in ubiquitin-directed proteasome- mediated degradation of the IkappaB members, thus permitting the release and nuclear translocation of the transcription factor, NF-kappaB. PMID: 16357866, 12659860 Expression of A20 inhibits TLR4-mediated NF-kappaB activation by regulating MEKK-1 kinase activity. PMID: 16357866, 12433373, 12433365 ectopic expression of SOCS1 in a macrophage cell line inhibits LPSinduced NF-kappaB activation. PMID: 16357866 A1 inhibits endothelial activation by inhibiting NF-kB activity. PMID: 16357866, 15864310 LPSinduced intracellular reactive oxygen species (ROS) mediate the formation of a complex between TRAF6 and ASK1 to facilitate activation of p38. Indirect PMID: 16357866, 15864310 LPSinduced intracellular reactive oxygen species (ROS) mediate the formation of a complex between TRAF6 and ASK1 to facilitate activation of p38. PMID: 16357866 SHIP1 also inhibits LPS-induced MAPK activation and IkB-a degradation. Indirect PMID: 16357866 The MyD88-dependent pathway is largely responsible for controlling the expression of inflammatory cytokines, such as TNF-alpha, IL-6 and IL-12, through activation of NF-kappaB. PMID: 16357866, 12154357, 12052830 Activation of PI3K also reduces MyD88-dependent production of the proinflammatory molecules IL-12 in dendritic cells and TNFa in monocytes. PMID: 16357866, 15699069 Mice that are deficient in Dok1 and Dok2 show an increase in TNFalpha and NO production in peritoneal and bone-marrow derived macrophages, as compared to wild-type cells. Indirect PMID: 16357866 The MyD88-dependent pathway is largely responsible for controlling the expression of inflammatory cytokines, such as TNF-alpha, IL-6 and IL-12, through activation of NF-kappaB. Indirect PMID: 16357866 The MyD88-dependent pathway is largely responsible for controlling the expression of inflammatory cytokines, such as TNF-alpha, IL-6 and IL-12, through activation of NF-kappaB. PMID: 16357866, 12154357, 12052830 Activation of PI3K also reduces MyD88-dependent production of the proinflammatory molecules IL-12 in dendritic cells and TNFa in monocytes. Indirect PMID: 16357866 activation of TRAF6 also results in the activation of PI3K and Akt. PMID: 16357866 The recruitment of these adaptor molecules to the receptor complex results in binding of TRAF6 and RIP1 to TRIF. Indirect PMID: 16357866 The recruitment of these adaptor molecules to the receptor complex results in binding of TRAF6 and RIP1 to TRIF, leading to the late-phase activation of NF-kappaB. PMID: 16357866, 12659860 Expression of A20 inhibits TLR4-mediated NF-kappaB activation by regulating MEKK-1 kinase activity. PMID: 16357866, 12433373, 12433365 ectopic expression of SOCS1 in a macrophage cell line inhibits LPSinduced NF-kappaB activation. PMID: 16357866 A1 inhibits endothelial activation by inhibiting NF-kB activity. Indirect PMID: 16357866, 15814722 The recruitment of these adaptor molecules to the receptor complex results in inding of TRAF6 and RIP1 to TRIF, leading to the late-phase activation of NF-kappaB, which contributes to the induction of IFN-beta. PMID: 16357866 TRAF family member-associated NF-kappaB activator (TANK) binding kinase 1 (TBK1) and IKKepsilon (also known as IKKi) interact with TRIF. Indirect PMID: 16357866, 12692549 TRAF family member-associated NF-kappaB activator (TANK) binding kinase 1 (TBK1) and IKKepsilon (also known as IKKi) interact with TRIF and mediate activation of IRF3. PMID: 16357866, 11244049 Once inside the nucleus, IRF3 controls IFNbeta transcription by recruiting the coactivators, p300 and CBP. PMID:16357866, 15611223 NF-kappaB activating kinase associating protein (NAP1) also interacts with TRIF and TBK1 to stimulate IFNbeta production through activation of IRF3. Indirect PMID:16357866, 15611223 NF-kappaB activating kinase associating protein (NAP1) also interacts with TRIF and TBK1 to stimulate IFNbeta production through activation of IRF3. Indirect PMID: 16357866, 15699069 Mice that are deficient in Dok1 and Dok2 show an increase in TNFalpha and NO production in peritoneal and bone-marrow derived macrophages, as compared to wild-type cells. PMID: 16357866, 15699069 Mice that are deficient in Dok1 and Dok2 show an increase in TNFalpha and NO production in peritoneal and bone-marrow derived macrophages, as compared to wild-type cells. PMID: 16357866, 10066820 inhibition of PI3K results in the induction of NOS. Indirect PMID: 16357866, 10066820 inhibition of PI3K results in the induction of NOS. PMID: 16357866, 10788611 PI3K has been shown to inhibit the expression of NOS2 in human astrocytes. PMID: 16357866 In unstimulated cells, Tollip forms a complex with IRAK. PMID: 16357866, 15935276, 9838078 PI3Ks are a family of kinases that catalyze the phosphorylation of phosphoinositides. The phosphorylated lipid products, phosphatidylinositol (PtdIns) 3,4-bisphosphate and PtdIns 3,4,5-triphosphate, then act as second messengers to activate downstream events, including activation of Akt. PMID: 16357866 SHIP1 negatively regulates LPS-induced activation of Akt downstream of PI3K. PMID: 16357866 The inhibitory effect of ST2 is the result of the interaction between its TIR domain and the TIR domains of MyD88 and TIRAP. PMID: 16357866, 15852007 The complex of RP105 and MD1 interacts with TLR4/MD2, impairing its ability to bind LPS. PMID: 16357866 The binding of IRAK4 to the receptor complex facilitates the transphosphorylation of IRAK1. PMID: 16357866, 10882101, 15836773 TAB2 links TAK1 to TRAF6 and facilitates the ubiquitination of TRAF6. PMID: 16357866 Although TAK1 phosphorylation occurs at the membrane and is dependent on the formation of the TRAF6–TAK1–TAB1–TAB2–TAB3 complex, it does not become active until the complex translocates to the cytoplasm. PMID; 16357866, 12242293 Although TAK1 phosphorylation occurs at the membrane and is dependent on the formation of the TRAF6–TAK1–TAB1–TAB2–TAB3 complex, it does not become active until the complex translocates to the cytoplasm. PMID: 16357866, 15107846 TRIAD3A, which contains structural features reminiscent of an E3 ubiquitinprotein ligase and promotes degradation of the receptor by targeting the receptor for ubiquitination and proteolytic degradation. Indirect PMID: 16357866, 15107846 TRIAD3A, which contains structural features reminiscent of an E3 ubiquitinprotein ligase and promotes degradation of the receptor by targeting the receptor for ubiquitination and proteolytic degradation. Indirect PMID: 16357866 TIFA promotes the oligomerization of TRAF6 and enhances the autoubiquitinating activity of TRAF6. PMID: 16357866 ubiquitin-directed proteasome-mediated degradation of the IkB members. PMID: 16357866, 11828002 FADD-/- MEFs stimulated with LPS demonstrate increased IkappaB-beta degradation compared to FADD+/+ cells, indicating that the role of FADD is upstream of IkappaB degradation. PMID: 16357866 SHIP1 also inhibits LPS-induced MAPK activation and IkB-a degradation. PMID: 16357866, 7628694 Activation of the IKKs leads to downstream phosphorylation of members of the inhibitor of NF-kB (IkB) family, resulting in ubiquitin-directed proteasome- mediated degradation of the IkB members, thus permitting the release and nuclear translocation of the transcription factor, NF-kB. Indirect PMID: 16357866, 15935276, 9838078 PI3Ks are a family of kinases that catalyze the phosphorylation of phosphoinositides. The phosphorylated lipid products, phosphatidylinositol (PtdIns) 3,4-bisphosphate and PtdIns 3,4,5-triphosphate, then act as second messengers to activate downstream events, including activation of Akt. PMID: 16357866, 15935276, 9838078 PI3Ks are a family of kinases that catalyze the phosphorylation of phosphoinositides. The phosphorylated lipid products, phosphatidylinositol (PtdIns) 3,4-bisphosphate and PtdIns 3,4,5-triphosphate, then act as second messengers to activate downstream events, including activation of Akt. PMID: 16357866 SHIP1 negatively regulates LPS-induced activation of Akt downstream of PI3K. PMID: 16357866, 11244049 IRF3 is a member of a family of transcription factors that are involved in the induction of type I IFNs that translocate to the nucleus upon phosphorylation and dimerization. PMID: 16357866, 11244049 IRF3 is a member of a family of transcription factors that are involved in the induction of type I IFNs that translocate to the nucleus upon phosphorylation and dimerization. Indirect PMID: 16357866, 12941697 activation of JNK is dependent on interaction of the scaffolding protein JNK-interacting protein 3 (JIP3) with the cytoplasmic domain of TLR4. PMID: 16357866 SHIP1 also inhibits LPS-induced MAPK activation and IkB-a degradation. PMID: 16357866, 12941697 activation of JNK is dependent on interaction of the scaffolding protein JNK-interacting protein 3 (JIP3) with the cytoplasmic domain of TLR4. Indirect PMID: 16357866, 11163183, 7937886 Tpl2 (also known as Cot) has been implicated in LPS-induced ERK activation in macrophages. Tpl2 has been shown to coordinate with the Ras pathway to induce activation of ERK in COS-1 monkey kidney cells. PMID: 16357866, 15699069 Overexpression of Dok1 or Dok2 inhibits LPS-induced ERK activation. SHIP1 also inhibits LPS-induced MAPK activation and IkB-a degradation. PMID: 16357866, 11244049 Once inside the nucleus, IRF3 controls IFNbeta transcription by recruiting the coactivators, p300 and CBP. PMID: 16357866, 11244049 Once inside the nucleus, IRF3 controls IFNbeta transcription by recruiting the coactivators, p300 and CBP. Indirect PMID: 16357866, 12692549 activation of IRF3, leading to the induction of IFNb. PMID: 16357866, 12356687 the MyD88-independent pathway induces expression of IFN-inducible genes, such as IP10 and glucocorticoid-attenuated response gene 16 (GARG16), through activation of the transcription factor, IFN regulatory factor 3 (IRF3). PMID: 16357866, 12356687 the MyD88-independent pathway induces expression of IFN-inducible genes, such as IP10 and glucocorticoid-attenuated response gene 16 (GARG16), through activation of the transcription factor, IFN regulatory factor 3 (IRF3). PMID: 16357866, 10880445 binding of FADD to the DD of MyD88 and subsequent recruitment of caspase 8. Indirect PMID: 16357866, 15852007 RP105-mediated inhibition of IL-8 production was the result of inhibition of NF-kB activity. Indirect PMID: 16357866, 15852007 RP105-mediated inhibition of IL-8 production was the result of inhibition of NF-kB activity. PMID: 16357866, 15866876 SIGIRR has recently been shown to interact with TLR4 through its TIR domain to attenuate recruitment of downstream signaling molecules. PMID: 16357866 TRIAD3 was identified as a RING-finger protein that interacts with the cytoplasmic tail of several TLRs, including TLR4. PMID: 16357866 IRAK-M can interact with both MyD88 and TRAF6. PMID: 16357866 IRAK-M can interact with both MyD88 and TRAF6. PMID: 16357866, 10880445 binding of FADD to the DD of MyD88 and subsequent recruitment of caspase 8. Indirect PMID: 16357866, 15100319 Inhibition of PI3K leads to a reduction in the activation of NF-kB and the MAPKs, p38 and p44/42. Indirect PMID: 16357866, 15100319 Inhibition of PI3K leads to a reduction in the activation of NF-kB and the MAPKs, p38 and p44/42.