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PMID: 18064347 TLR4 is activated by endogenous ligands, such as heat shock protein 60 (HSP60), HSP70, fibronectin, hyaluronic acid, fibrinogen and heparan sulfate. PMID: 18064347, 10644670, 11274165 TLR4 can also recognize taxol (a strong antitumor agent in humans) derived from Taxus brevifolia, and a respiratory syncytial virus fusion protein. PMID: 18064347 TLR4 is activated by endogenous ligands, such as heat shock protein 60 (HSP60), HSP70, fibronectin, hyaluronic acid, fibrinogen and heparan sulfate. PMID: 18064347 TLR4 is activated by endogenous ligands, such as heat shock protein 60 (HSP60), HSP70, fibronectin, hyaluronic acid, fibrinogen and heparan sulfate. PMID: 18064347 TLR4 is activated by endogenous ligands, such as heat shock protein 60 (HSP60), HSP70, fibronectin, hyaluronic acid, fibrinogen and heparan sulfate. PMID: 18064347 TLR4 is activated by endogenous ligands, such as heat shock protein 60 (HSP60), HSP70, fibronectin, hyaluronic acid, fibrinogen and heparan sulfate. PMID: 18064347, 11274165 LPS is generally bound to LPS-binding protein (LBP) present in the serum, this complex is firstly recognized by CD14 receptor, strongly expressed in peripheral blood monocytes and macrophages. PMID: 18064347, 11274165 LPS is generally bound to LPS-binding protein (LBP) present in the serum, this complex is firstly recognized by CD14 receptor, strongly expressed in peripheral blood monocytes and macrophages. PMID: 18064347, 11274165 Once bound to CD14, LPS comes in close proximity with TLR4; however the efficient triggering of an inflammatory response requires the expression of the secreted protein MD-2 PMID: 18064347, 11274165 Once bound to CD14, LPS comes in close proximity with TLR4; however the efficient triggering of an inflammatory response requires the expression of the secreted protein MD-2 PMID: 18064347, 14625549 TLR5 recognizes a flagellin portion derived from Gram-positive and negative bacteria. PMID: 18064347, 15345224, 14993594, 12900525, 14563635 TLR9 senses DNA from Murine Cytomegalovirus (MCMV) and Herpes Simplex virus 1 and 2. PMID: 18064347, 14976262, 15804288, 15661881 TLR7 responds to ssRNA producing interferon type I (IFN type I) and pro-inflammatory cytokines. indirect PMID: 18064347, 14976262, 15804288, 15661881 TLR7 responds to ssRNA producing interferon type I (IFN type I) and pro-inflammatory cytokines. PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7. indirect PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7. indirect PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7. indirect PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7. indirect PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7. indirect PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7. indirect PMID: 18064347, 15361868, 16006187 TLR7 and TLR8 recognize viral and non-viral ssRNA and activate cytokine production through interferon regulatory factor 3 (IRF3) and IRF7. PMID: 18064347, 16095970, 15829275, 15254159 Adequate host defense against viral infections involves rapid pathogen recognition by TLR3, TLR7, TLR8 and TLR9 among other PRRs. The viral PAMPs recognized by these receptors include: double-stranded RNA (dsRNA), single-stranded RNA (ssRNA) and double-stranded DNA (dsDNA) PMID: 18064347 when TLR2,4 and 5 are activated MYD88 is recruited to TLR/TIR domain to induce pro inflammatory cytokine through a classical signal pathway. PMID: 18064347 When TLR2,4 and 5 are activated MYD88 is recruited to TLR/TIR domain to induce pro inflammatory cytokine through a classical signal pathway. PMID: 18064347 When TLR2,4 and 5 are activated MYD88 is recruited to TLR/TIR domain to induce pro inflammatory cytokine through a classical signal pathway. PMID: 18064347 During viral recognition in endosome TLR7, 8 and 9 use the cytoplasmic adaptor molecule MYD88. PMID: 18064347 During viral recognition in endosome TLR7, 8 and 9 use the cytoplasmic adaptor molecule MYD88. PMID: 18064347 During viral recognition in endosome TLR7, 8 and 9 use the cytoplasmic adaptor molecule MYD88. PMID: 18064347 When TLR2, 4 and 5 are activated, MyD88 is recruited to the TLR/TIR domain to induce pro-inflammatory cytokine production through a classical signaling pathway. In this pathway the IKK family of proteins is activated in a process that involves IRAK-1 and TRAF6. PMID: 18064347 When TLR2, 4 and 5 are activated, MyD88 is recruited to the TLR/TIR domain to induce pro-inflammatory cytokine production through a classical signaling pathway. In this pathway the IKK family of proteins is activated in a process that involves IRAK-1 and TRAF6. PMID: 18064347 The IKK complex catalyzes IκBα phosphorylation and degradation by the proteasome, therefore allowing NFκB to translocate into the nucleus. indirect PMID: 18064347 When TLR2, 4 and 5 are activated, MyD88 is recruited to the TLR/TIR domain to induce pro-inflammatory cytokine production through a classical signaling pathway. In this pathway the IKK family of proteins is activated in a process that involves IRAK-1 and TRAF6. indirect PMID: 18064347 When TLR2, 4 and 5 are activated, MyD88 is recruited to the TLR/TIR domain to induce pro-inflammatory cytokine production through a classical signaling pathway. In this pathway the IKK family of proteins is activated in a process that involves IRAK-1 and TRAF6. PMID: 18064347 The IKK complex catalyzes IκBα phosphorylation and degradation by the proteasome, therefore allowing NFκB to translocate into the nucleus. PMID: 18064347 The IKK complex catalyzes IκBα phosphorylation and degradation by the proteasome, therefore allowing NFκB to translocate into the nucleus. PMID: 18064347 Once in the nucleus, NFκB regulates the expression of pro-inflammatory cytokines and adhesion molecules. PMID: 18064347 Once in the nucleus, NFκB regulates the expression of pro-inflammatory cytokines and adhesion molecules. PMID: 18064347 In addition, TLR2 and 4 uses a MyD88-independent pathway that involves PI3K and TRIF recruitment to the TLR/TIR domain. PMID: 18064347 In addition, TLR2 and 4 uses a MyD88-independent pathway that involves PI3K and TRIF recruitment to the TLR/TIR domain. PMID: 18064347, 11431423, 12077222 the association between TLR1 and TLR6 which were demonstrated to form heterodimeric complexes with TLR2. PMID: 18064347, 11431423, 12077222 TLR6 association with TLR2 induced recognition of diacylated lipopeptide but TLR1-TLR2 heterodimer binds preferentially triacylated lipopeptides. PMID: 18064347, 11431423, 12077222 TLR6 association with TLR2 induced recognition of diacylated lipopeptide but TLR1-TLR2 heterodimer binds preferentially triacylated lipopeptides. indirect PMID: 18064347 TLR4 activates a TRIF-dependent pathway that induces the activation of IRF-3 and subsequently the production of type I IFN in response to LPS. PMID: 18064347, 12368275, 14519765 TLR4 utilizes the adaptors TRIF and TRAM independently of Mai and MyD88 to initiate the late phase of NFκB activation and also to induce the expression of IFN-ß and other IFN-inducible genes via the transcription factor IRF-3. PMID: 18064347 TLR4 activates a TRIF-dependent pathway that induces the activation of IRF-3 and subsequently the production of type I IFN in response to LPS. PMID: 18064347 TLR3 triggers a TIR domain-containing adaptor inducing IFN-β (TRIF) signaling pathway independent of MyD88 recruitment. indirect PMID: 18064347 TLR3 can also regulate IFNα/β production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation. indirect PMID: 18064347 TLR3 can also regulate IFNα/β production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation. indirect PMID: 18064347 TLR3 can also regulate IFNα/β production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation. indirect PMID: 18064347 TLR3 can also regulate IFNα/β production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation. PMID: 18064347 TLR3 can also regulate IFNα/β production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation. PMID: 18064347 TLR3 can also regulate IFNα/β production by IRFs, through a TRIF-dependent pathway that may also involve PI3K or TBK1/IKK-epsilon activation. PMID: 18064347 The soluble product sTLR4 is an alternative splice variant of TLR4 that was shown to be expressed as a mechanism to inhibit LPS -mediated TNFα production and NFκB activation, blocking MD-2 recruitment to the TLR4-CD14 complex. indirect PMID: 18064347 The soluble product sTLR4 is an alternative splice variant of TLR4 that was shown to be expressed as a mechanism to inhibit LPS -mediated TNFα production and NFκB activation, blocking MD-2 recruitment to the TLR4-CD14 complex. PMID: 18064347, 12538665 The mechanism by which MyD88s reverts inflammation involves IRAK-4 sequestration by MyD88s that prevents further phosphorylation of IRAK-4 and IRAK-1 and activation of NFκB. PMID: 18064347, 12154357, 12052830 PI3K has been also implicated in TLRs signaling, suppressing both MAPKs and NFκB in response to LPS, thereby decreasing TNFα production. PMID: 18064347, 15004556 A possible mechanism for ST2L immune modulation involves its interaction with molecular adaptors of TLR/IL-1 inflammatory pathways. ST2L can sequestrate MyD88 and Mai through their TIR domains, and therefore can block the effect of TLR4-mediated NFκB activation indirect PMID: 18064347 The soluble product sTLR4 is an alternative splice variant of TLR4 that was shown to be expressed as a mechanism to inhibit LPS -mediated TNFα production and NFκB activation, blocking MD-2 recruitment to the TLR4-CD14 complex. PMID: 18064347, 12154357, 12052830 PI3K has been also implicated in TLRs signaling, suppressing both MAPKs and NFκB in response to LPS, thereby decreasing TNFα production. PMID: 18064347, 15502848 agonist activation of TLR3 may promote tyrosine phosphorylation that allows phosphatidylinositol 3-kinase (PI3K) recruitment, Akt activation and finally IRF-3 phosphorylation. PMID: 18064347, 15502848 agonist activation of TLR3 may promote tyrosine phosphorylation that allows phosphatidylinositol 3-kinase (PI3K) recruitment, Akt activation and finally IRF-3 phosphorylation. indirect PMID: 18064347, 15502848 agonist activation of TLR3 may promote tyrosine phosphorylation that allows phosphatidylinositol 3-kinase (PI3K) recruitment, Akt activation and finally IRF-3 phosphorylation. PMID: 18064347, 15502848 agonist activation of TLR3 may promote tyrosine phosphorylation that allows phosphatidylinositol 3-kinase (PI3K) recruitment, Akt activation and finally IRF-3 phosphorylation. PMID: 18064347 A crucial event in pro-inflammatory signaling activation is the interaction of IRAK-4 with MyD88-ID domain that promotes, after recruitment to the receptor TIR domain, the phosphorylation of IRAK-1. PMID: 18064347 A crucial event in pro-inflammatory signaling activation is the interaction of IRAK-4 with MyD88-ID domain that promotes, after recruitment to the receptor TIR domain, the phosphorylation of IRAK-1. PMID: 18064347, 12150927 IRAK-M and IRAK-2 block pro-inflammatory cytokine expression by dissociating the complex formed by MyD88-IRAK-l/-4 and IRAK-TRAF6. IRAK-M -/- mice show an over-production of inflammatory cytokines in response to LPS and bacterial DNA-like CpG motifs. PMID: 18064347 A crucial event in pro-inflammatory signaling activation is the interaction of IRAK-4 with MyD88-ID domain that promotes, after recruitment to the receptor TIR domain, the phosphorylation of IRAK-1. PMID: 18064347, 12538665 The mechanism by which MyD88s reverts inflammation involves IRAK-4 sequestration by MyD88s that prevents further phosphorylation of IRAK-4 and IRAK-1 and activation of NFκB. PMID: 18064347, 10854325 Tollip is recruited to the TIR domain and decreases IRAK-1 phosphorylation upon LPS activation. IRAK-1 activation by MyD88 promotes Tollip dissociation from the TIR domain. PMID: 18064347 Once IRAK-1 is phosphorylated TRAF6 is recruited to the TLR complex. PMID: 18064347, 12150927 IRAK-M and IRAK-2 block pro-inflammatory cytokine expression by dissociating the complex formed by MyD88-IRAK-l/-4 and IRAK-TRAF6. IRAK-M -/- mice show an over-production of inflammatory cytokines in response to LPS and bacterial DNA-like CpG motifs . PMID: 18064347, 11259596 IRAK-1 and TRAF6 dissociate from the TIR/MyD88/IRAK-4 complex and interact with membrane-associated proteins, such as TAK1 (transforming growth factor-(ß-activated kinase 1), TAB1 (transforming growth factor-(ß-activated protein kinase 1-binding protein 1) and TAB2 that are part of the multicomplex IRAK-1-TRAF6-TAK1-TAB1-TAB2. PMID: 18064347, 11259596 IRAK-1 and TRAF6 dissociate from the TIR/MyD88/IRAK-4 complex and interact with membrane-associated proteins, such as TAK1 (transforming growth factor-(ß-activated kinase 1), TAB1 (transforming growth factor-(ß-activated protein kinase 1-binding protein 1) and TAB2 that are part of the multicomplex IRAK-1-TRAF6-TAK1-TAB1-TAB2. PMID: 18064347, 12242293 When TAK1 and TAB2 become phosphorylated they induce IRAK-1 dissociation from the complex and further IKKs and MAPKs activation. PMID: 18064347, 12242293 When TAK1 and TAB2 become phosphorylated they induce IRAK-1 dissociation from the complex and further IKKs and MAPKs activation. PMID: 18064347, 15147900, 11460167 Recent studies showed that TRAF6 can bind ubiquitin-conjugating enzymes Ubcl3 and UevlA, that are critical in the activation of TAK1 -mediated phosphorylation of IKK and MKK (MAPK Kinases) PMID: 18064347, 15147900, 11460167 Recent studies showed that TRAF6 can bind ubiquitin-conjugating enzymes Ubcl3 and UevlA, that are critical in the activation of TAK1 -mediated phosphorylation of IKK and MKK (MAPK Kinases) PMID: 18064347, 15147900, 11460167 Recent studies showed that TRAF6 can bind ubiquitin-conjugating enzymes Ubcl3 and UevlA, that are critical in the activation of TAK1 -mediated phosphorylation of IKK and MKK (MAPK Kinases). PMID: 18064347, 12154357, 12052830 PI3K has been also implicated in TLRs signaling, suppressing both MAPKs and NFκB in response to LPS, thereby decreasing TNFα production. PMID: 18064347 The IKK complex catalyzes IκBα phosphorylation and degradation by the proteasome, therefore allowing NFκB to translocate into the nucleus. PMID: 18064347 TRAM, like Mai, acts as a bridge to couple TRIF to TLR4 and is absolutely required for TLR4 mediated responses. indirect PMID: 18064347 TLR4 activation by LPS may induce the expression of the TRIF-related adaptor molecule (TRAM/TICAM-2) that binds to TLR4 and to TRIF. indirect PMID: 18064347 TLR4 activation by LPS may induce the expression of the TRIF-related adaptor molecule (TRAM/TICAM-2) that binds to TLR4 and to TRIF. indirect PMID: 18064347, 12368275, 14519765 TLR4 utilizes the adaptors TRIF and TRAM independently of Mai and MyD88 to initiate the late phase of NFκB activation and also to induce the expression of IFN-ß and other IFN-inducible genes via the transcription factor IRF-3. PMID: 18064347, 12538665 The mechanism by which MyD88s reverts inflammation involves IRAK-4 sequestration by MyD88s that prevents further phosphorylation of IRAK-4 and IRAK-1 and activation of NFκB. PMID: 18064347 PI3K is an enzyme that catalyzes the phosphorylation of phosphatidylinositol 4,5-bisphosphate (PIP2) to phosphatidylinositol 3,4,5-trisphosphate (PIP3). PMID: 18064347, 11101877 Stimulation of TLR2 expressing cells with Staphylococcus aureus promotes PI3K recruitment to the TIR domain and induces transactivation of the NFκB subunit p65 by a mechanism that seems to be independent of IκBα proteasomic degradation. indirect PMID: 18064347, 11101877 Stimulation of TLR2 expressing cells with Staphylococcus aureus promotes PI3K recruitment to the TIR domain and induces transactivation of the NFκB subunit p65 by a mechanism that seems to be independent of IκBα proteasomic degradation. PMID: 18064347, 10854325 Tollip is recruited to the TIR domain and decreases IRAK-1 phosphorylation upon LPS activation. IRAK-1 activation by MyD88 promotes Tollip dissociation from the TIR domain. indirect PMID: 18064347, 10854325 Tollip is recruited to the TIR domain and decreases IRAK-1 phosphorylation upon LPS activation. IRAK-1 activation by MyD88 promotes Tollip dissociation from the TIR domain. PMID: 18064347, 12514169, 12527755 NOD2 protein is constituted by two caspase recruitment domains (CARD), a NOD region and a tripartite domain, consisting of a C-terminal LRR. This last domain recognizes and reacts to the bacterial component muramyl dipeptide (MDP), and is the site with major genetic variability. PMID: 18064347, 15004556 A possible mechanism for ST2L immune modulation involves its interaction with molecular adaptors of TLR/IL-1 inflammatory pathways. ST2L can sequestrate MyD88 and Mai through their TIR domains, and therefore can block the effect of TLR4-mediated NFκB activation indirect PMID: 18064347, 11359817 In LPS-activated macrophages, ST2s downregulates TLR4 mRNA expression. PMID: 18064347, 12925853, 15866876 SIGIRR interacts with IL-1R and TLR4 in a ligand-dependent manner and inhibits their signaling. PMID: 18064347, 12925853, 15866876 SIGIRR interacts with IL-1R and TLR4 in a ligand-dependent manner and inhibits their signaling. PMID: 18064347, 12925853, 15866876 SIGIRR interacts with IL-1R and TLR4 in a ligand-dependent manner and inhibits their signaling. PMID: 18064347, 15004556 A possible mechanism for ST2L immune modulation involves its interaction with molecular adaptors of TLR/IL-1 inflammatory pathways. ST2L can sequestrate MyD88 and Mai through their TIR domains, and therefore can block the effect of TLR4-mediated NFκB activation