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c 3.24 3.7887 3.4544 -0.7608 -7.8409 8.8103 c 0.0483 5.5259 -4.3434 2.8195 -7.3185 3.9889 c -0.165 6.88 2.4396 3.6618 -5.6223 3.2188 c -3.0769 0.9931 -7.0254 2.7728 -9.6003 3.4432 l 12.8455 -3.4945 c 4.7898 -1.7598 0.3068 -3.3597 6.3871 9.8147 c 5.5407 1.664 1.4772 4.7998 1.7274 7.8523 c 6.8289 2.2753 4.4157 -1.0751 1.4814 6.08 c 0.0423 3.0898 0.6019 7.2116 0.4764 9.7476 l 0.4749 -12.6987 c -0.2796 -4.8764 -3.2648 -1.3155 11.7884 -2.7443 c 3.3761 -4.4975 5.2562 0.1471 8.386 0.8639 c 4.3855 -5.4739 0.2895 -4.3263 6.5377 0.5388 c 3.1029 0.9165 7.3975 1.6842 9.895 2.5812 z" /> </svg> PMID: 17635639 TLR4 can also initiate a Mal/MyD88-independent signalling pathway through the recruitment of TRAM and TRIF. PMID: 17635639, 16751103 In the case of TLR2 and TLR4, MyD88 recruitment requires Mal, whereas the other TLRs and the IL-1R signal independently of Mal. PMID: 17635639 TLR2 responds to lipoproteins, TLR3 to viral double-stranded RNA, TLR4 to lipopolysaccharide (LPS), TLR5 to flagellin, TLR7 and TLR8 to viral single stranded RNA, and TLR9 to unmethylated CpG islands of bacterial and viral DNA. PMID: 17635639 Upon LPS-binding (mediated by MD-2 and CD14) to TLR4 and subsequent TLR4 clustering, Mal, MyD88, IRAK-1, Tollip and IRAK-4 are recruited to the cytoplasmic part of the receptor via TLR4/MyD88 TIR–TIR interactions PMID: 17635639 Upon LPS-binding (mediated by MD-2 and CD14) to TLR4 and subsequent TLR4 clustering, Mal, MyD88, IRAK-1, Tollip and IRAK-4 are recruited to the cytoplasmic part of the receptor via TLR4/MyD88 TIR–TIR interactions PMID: 17635639 TLR4 can also initiate a Mal/MyD88-independent signalling pathway through the recruitment of TRAM and TRIF. PMID: 17635639 Binding of MyD88 to TLR4 allows the recruitment of IL-1R associated kinase (IRAK)-1 and IRAK-4 through the death domains (DD) of both kinases and the DD and intermediate domain of MyD88. PMID: 17635639, 16751103 In the case of TLR2 and TLR4, MyD88 recruitment requires Mal, whereas the other TLRs and the IL-1R signal independently of Mal. PMID: 17635639 Upon LPS-binding (mediated by MD-2 and CD14) to TLR4 and subsequent TLR4 clustering, Mal, MyD88, IRAK-1, Tollip and IRAK-4 are recruited to the cytoplasmic part of the receptor via TLR4/MyD88 TIR–TIR interactions PMID: 17635639, 16751103 In the case of TLR2 and TLR4, MyD88 recruitment requires Mal, whereas the other TLRs and the IL-1R signal independently of Mal. PMID: 17635639, 16751103 In the case of TLR2 and TLR4, MyD88 recruitment requires Mal, whereas the other TLRs and the IL-1R signal independently of Mal. PMID: 17635639, 16751103 In the case of TLR2 and TLR4, MyD88 recruitment requires Mal, whereas the other TLRs and the IL-1R signal independently of Mal. PMID: 17635639, 16751103 In the case of TLR2 and TLR4, MyD88 recruitment requires Mal, whereas the other TLRs and the IL-1R signal independently of Mal. PMID: 17635639 TLR2 responds to lipoproteins, TLR3 to viral double-stranded RNA, TLR4 to lipopolysaccharide (LPS), TLR5 to flagellin, TLR7 and TLR8 to viral single stranded RNA, and TLR9 to unmethylated CpG islands of bacterial and viral DNA. PMID: 17635639 TLR2 responds to lipoproteins, TLR3 to viral double-stranded RNA, TLR4 to lipopolysaccharide (LPS), TLR5 to flagellin, TLR7 and TLR8 to viral single stranded RNA, and TLR9 to unmethylated CpG islands of bacterial and viral DNA. PMID: 17635639 TLR2 responds to lipoproteins, TLR3 to viral double-stranded RNA, TLR4 to lipopolysaccharide (LPS), TLR5 to flagellin, TLR7 and TLR8 to viral single stranded RNA, and TLR9 to unmethylated CpG islands of bacterial and viral DNA. PMID: 17635639 TLR2 responds to lipoproteins, TLR3 to viral double-stranded RNA, TLR4 to lipopolysaccharide (LPS), TLR5 to flagellin, TLR7 and TLR8 to viral single stranded RNA, and TLR9 to unmethylated CpG islands of bacterial and viral DNA. PMID: 17635639, 16751103 In the case of TLR2 and TLR4, MyD88 recruitment requires Mal, whereas the other TLRs and the IL-1R signal independently of Mal. PMID: 17635639, 16751103 In the case of TLR2 and TLR4, MyD88 recruitment requires Mal, whereas the other TLRs and the IL-1R signal independently of Mal. PMID: 17635639 TLR2 responds to lipoproteins, TLR3 to viral double-stranded RNA, TLR4 to lipopolysaccharide (LPS), TLR5 to flagellin, TLR7 and TLR8 to viral single stranded RNA, and TLR9 to unmethylated CpG islands of bacterial and viral DNA. PMID: 17635639 TLR2 responds to lipoproteins, TLR3 to viral double-stranded RNA, TLR4 to lipopolysaccharide (LPS), TLR5 to flagellin, TLR7 and TLR8 to viral single stranded RNA, and TLR9 to unmethylated CpG islands of bacterial and viral DNA. PMID: 17635639, 11960013, 15084582, 14625308 close proximity in the receptor complex enables IRAK-4 to phosphorylate IRAK-1, leading to its activation and IRAK–1 autophosphorylation. PMID: 17635639, 11960013, 15084582, 14625308 close proximity in the receptor complex enables IRAK-4 to phosphorylate IRAK-1, leading to its activation and IRAK–1 autophosphorylation. PMID: 17635639 Active IRAK–1 also phosphorylates Tollip, supposedly a silencer for quiescent IRAK-1, which subsequently leaves the receptor complex PMID: 17635639 Active IRAK–1 also phosphorylates Tollip, supposedly a silencer for quiescent IRAK-1, which subsequently leaves the receptor complex PMID: 17635639, 15492226 IRAK-1 in turn interacts with the signalling molecule TRAF6 and TIFA, which is an adaptor protein that has been suggested to promote the oligomerization and ubiquitination of TRAF6. PMID: 17635639, 9466656 The IRAK-1/TRAF6/TIFA complex then leaves the receptor complex but remains at the membrane where it interacts with a preformed (but inactive) complex consisting of the mitogen activated protein kinase (MAPK) kinase kinase TAK1 and the adaptor molecules TAB1 and TAB2 or TAB3.. PMID: 17635639, 9466656 The IRAK-1/TRAF6/TIFA complex then leaves the receptor complex but remains at the membrane where it interacts with a preformed (but inactive) complex consisting of the mitogen activated protein kinase (MAPK) kinase kinase TAK1 and the adaptor molecules TAB1 and TAB2 or TAB3.. PMID: 17635639 After phosphorylation of TAK1 and TAB2, the newly formed TRAF6-TAB2/3-TAK1-TAB1 complex migrates to the cytosol while IRAK-1 has been suggested to remain at the membrane and to disappear by proteasomal degradation. PMID: 17635639 After phosphorylation of TAK1 and TAB2, the newly formed TRAF6-TAB2/3-TAK1-TAB1 complex migrates to the cytosol while IRAK-1 has been suggested to remain at the membrane and to disappear by proteasomal degradation. PMID: 17635639 After phosphorylation of TAK1 and TAB2, the newly formed TRAF6-TAB2/3-TAK1-TAB1 complex migrates to the cytosol while IRAK-1 has been suggested to remain at the membrane and to disappear by proteasomal degradation. PMID: 17635639, 15896328 A redistribution of IRAK-1 from the receptor complex to the nucleus has also been shown upon receptor triggering, but the function of nuclear IRAK-1 remains speculative. PMID: 17635639 TIFA promotes the oligomerization and activation of TRAF6, leading to TRAF6 K63-linked polyubiquitination and subsequent TAK1 activation. PMID: 17635639 TIFA promotes the oligomerization and activation of TRAF6, leading to TRAF6 K63-linked polyubiquitination and subsequent TAK1 activation. indirect PMID: 17635639, 11057907, 11460167 Active TAK1 then leads to the downstream activation of IκB kinases (IKK) and JNK or p38 MAPKs. indirect PMID: 17635639, 11057907, 11460167 Active TAK1 then leads to the downstream activation of IκB kinases (IKK) and JNK or p38 MAPKs. indirect PMID: 17635639, 11057907, 11460167 Active TAK1 then leads to the downstream activation of IκB kinases (IKK) and JNK or p38 MAPKs. PMID: 17635639 IKKs eventually activate NF-κB by phosphorylating the NF-κB inhibitory protein IκBα, leading to its ubiquitination and proteasome-dependent degradation, whereas JNK and p38 further contribute to the innate immune response by phosphorylating and activating several other transcription factors. PMID: 17635639 IKKs eventually activate NF-κB by phosphorylating the NF-κB inhibitory protein IκBα, leading to its ubiquitination and proteasome-dependent degradation, whereas JNK and p38 further contribute to the innate immune response by phosphorylating and activating several other transcription factors. PMID: 17635639 IKKs eventually activate NF-κB by phosphorylating the NF-κB inhibitory protein IκBα, leading to its ubiquitination and proteasome-dependent degradation, whereas JNK and p38 further contribute to the innate immune response by phosphorylating and activating several other transcription factors PMID: 17635639 IKKs eventually activate NF-κB by phosphorylating the NF-κB inhibitory protein IκBα, leading to its ubiquitination and proteasome-dependent degradation, whereas JNK and p38 further contribute to the innate immune response by phosphorylating and activating several other transcription factors PMID: 17635639 IKKs eventually activate NF-κB by phosphorylating the NF-κB inhibitory protein IκBα, leading to its ubiquitination and proteasome-dependent degradation, whereas JNK and p38 further contribute to the innate immune response by phosphorylating and activating several other transcription factors PMID: 17635639 Pellino proteins associate with IRAK-1, TRAF6 and TAK1 and become phosphorylated by IRAK-1. PMID: 17635639, 12874243 Based on the observation that Pellino-3 can simultaneously interact with endogenous IRAK-1, TRAF6 and TAK1 upon IL-1 stimulation, it was hypothesized that Pellino proteins might act as scaffold proteins that regulate signalling branch-points in TLR/IL-1R signalling to NF-κB and MAPKs. PMID: 17635639 Pellino proteins associate with IRAK-1, TRAF6 and TAK1 and become phosphorylated by IRAK-1. PMID: 17635639 Pellino proteins associate with IRAK-1, TRAF6 and TAK1 and become phosphorylated by IRAK-1. PMID: 17635639, 12874243 Based on the observation that Pellino-3 can simultaneously interact with endogenous IRAK-1, TRAF6 and TAK1 upon IL-1 stimulation, it was hypothesized that Pellino proteins might act as scaffold proteins that regulate signalling branch-points in TLR/IL-1R signalling to NF-κB and MAPKs. PMID: 17635639 Pellino-1 and -2 also induce IRAK-1 polyubiquitination. PMID: 17635639, 12874243 Pellino-3 was also shown to bind the Ser/Thr kinase NIK. indirect PMID: 17635639, 16951688 Pellino-1 was recently found to interact with Smad6, an anti-inflammatory protein induced by TGF-β. indirect PMID: 17635639, 16951688 This Pellino-1/Smad6 interaction completely abrogat-ed the formation of the Pellino-1/IRAK-1/TRAF6 signalling complex induced by IL-1. PMID: 17635639, 16951688 the same group also reported an interaction between Pellino-1 and the TLR/IL-1R adaptor protein MyD88. PMID: 17635639, 15213237 Pellino-2 was also picked up via phage display as a Bcl-10 interacting protein and shown to interact with Bcl-10 in RAW264.7 macrophages treated with LPS. indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression indirect PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-κB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression PMID: 17635639, 15917247, 16884718, 12496252, 12370331, 12860405, 16951688, 15917247 all mammalian Pellino proteins were shown to interact with IRAK-1 and IRAK-4. PMID: 17635639, 15917247, 16884718, 12496252, 12370331, 12860405, 16951688, 15917247 all mammalian Pellino proteins were shown to interact with IRAK-1 and IRAK-4. PMID: 17635639, 15917247, 16884718, 12496252, 12370331, 12860405, 16951688, 15917247 all mammalian Pellino proteins were shown to interact with IRAK-1 and IRAK-4. PMID: 17635639, 15917247, 16884718, 12496252, 12370331, 12860405, 16951688, 15917247 all mammalian Pellino proteins were shown to interact with IRAK-1 and IRAK-4. PMID: 17635639, 15917247, 16884718, 12496252, 12370331, 12860405, 16951688, 15917247 all mammalian Pellino proteins were shown to interact with IRAK-1 and IRAK-4. PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1. PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1. PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1. PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1. PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1. PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1. PMID: 17635639, 15896328 A redistribution of IRAK-1 from the receptor complex to the nucleus has also been shown upon receptor triggering, but the function of nuclear IRAK-1 remains speculative.