Original Literature | Model OverView |
---|---|
Publication
Title
Pellino proteins: novel players in TLR and IL-1R signalling.
Affiliation
Unit of Molecular Signal Transduction in Inflammation, Department for MolecularBiomedical Research, VIB, Ghent, Belgium.
Abstract
Members of the Toll-like receptor (TLR) and interleukin-1 receptor (IL-1R)family play important roles in immunity and inflammation. They initiate commonintracellular signalling cascades leading to the activation of nuclear factor-?B(NF-?B) and other transcription factors that stimulate the expression of avariety of genes that shape an appropriate immune response. TLR/IL-1R signallinginvolves multiple proteinprotein interactions, but the mechanisms that regulatethese interactions are still largely unclear. In this context, Pellino proteinshave been suggested to function as evolutionary conserved scaffold proteins inTLR/IL-1R signalling. However, recently Pellino proteins were also proposed tofunction as novel ubiquitin ligases for IL-1R associated kinase 1 (IRAK-1). Herewe review our current knowledge on the expression, biological role and mechanismof action of Pellino proteins in TLR/IL-1R-induced signalling.
PMID
17635639
|
Entity
Process
Elk-1{active}
--
MO000000038
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TRANSPATH | MO000000038 |
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c-Jun
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TRANSPATH | MO000000049 |
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TRANSPATH | MO000016574 |
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TRANSPATH | MO000019479 |
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TRANSPATH | MO000039077 |
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--
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TRANSPATH | MO000041419 |
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TRANSPATH | MO000041420 |
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TRANSPATH | MO000041425 |
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TRANSPATH | MO000041433 |
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TRANSPATH | MO000041446 |
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--
--
csml-variable:Double
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IRAK1
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e30
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LPS:TLR4:MD2:TIRAP:MYD88:IRAK1:IRAK4
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e31
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e4
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TRANSPATH | MO000000022 |
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TRANSPATH | MO000000023 |
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--
csml-variable:Double
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IRAK1{p}{ub}:TRAF6:TIFA:TAK1:TAB1:TAB2:pellino{p}
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e73
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csml-variable:Double
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0
--
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e74
cso30:c:Complex
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--
csml-variable:Double
m76
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e75
cso30:c:Complex
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e76
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--
csml-variable:Double
m78
0
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0
--
TGF-beta
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e77
cso30:c:Protein
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--
csml-variable:Double
m79
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e78
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--
csml-variable:Double
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e79
cso30:c:Complex
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--
csml-variable:Double
m81
0
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0
--
--
e8
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--
--
csml-variable:Double
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0
--
ERK{active}
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e80
cso30:c:Protein
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csml-variable:Double
m83
10
infinite
0
TRANSPATH | MO000000011 |
--
c-Jun{active}
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e81
cso30:c:Protein
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csml-variable:Double
m85
10
infinite
0
InterPro | IPR002112 |
TRANSPATH | MO000000049 |
--
CREB{active}
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e83
cso30:c:Protein
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csml-variable:Double
m88
10
infinite
0
InterPro | IPR003102 |
TRANSPATH | MO000017189 |
--
CHOP
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e84
cso30:c:Protein
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csml-variable:Double
m89
0
infinite
0
--
CHOP{active}
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e85
cso30:c:Protein
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csml-variable:Double
m90
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infinite
0
--
csml-variable:Double
m91
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infinite
0
--
pellino3:IRAK1
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e87
cso30:c:Complex
cso30:i:CC_Cytosol
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--
csml-variable:Double
m92
0
infinite
0
--
pellino2:IRAK1
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e88
cso30:c:Complex
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--
csml-variable:Double
m93
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infinite
0
--
Pellino2:IRAK4
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e89
cso30:c:Complex
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--
--
csml-variable:Double
m94
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0
--
--
e9
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--
--
--
csml-variable:Double
m9
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0
--
pellino2:TRAF6
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e90
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--
csml-variable:Double
m95
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0
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pellino1:TRAF6
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e91
cso30:c:Complex
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--
csml-variable:Double
m96
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0
--
Pellino3:TRAF6
--
e92
cso30:c:Complex
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--
csml-variable:Double
m97
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0
--
pellino1:TAK1
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e93
cso30:c:Complex
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--
csml-variable:Double
m98
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0
--
TAK1:pellino2
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e94
cso30:c:Complex
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--
csml-variable:Double
m99
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0
--
TAK1:pellino3
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e95
cso30:c:Complex
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--
csml-variable:Double
m100
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--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c1 : 1
stoichiometry:c2 : 1
stoichiometry:c3 : 1
m5*m3964*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c29 : 1
stoichiometry:c30 : 1
stoichiometry:c31 : 1
m11*m6810*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c32 : 1
stoichiometry:c33 : 1
stoichiometry:c34 : 1
m20*m1572*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c35 : 1
stoichiometry:c36 : 1
stoichiometry:c37 : 1
m6810*m6*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c38 : 1
stoichiometry:c39 : 1
stoichiometry:c40 : 1
m22*m1572*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c41 : 1
stoichiometry:c42 : 1
stoichiometry:c43 : 1
m12*m1572*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c44 : 1
stoichiometry:c45 : 1
stoichiometry:c46 : 1
m13*m1572*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c47 : 1
stoichiometry:c48 : 1
stoichiometry:c49 : 1
m15*m1572*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c50 : 1
stoichiometry:c51 : 1
stoichiometry:c52 : 1
m17*m1572*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c53 : 1
stoichiometry:c54 : 1
stoichiometry:c55 : 1
m11*m19005*0.1
nodelay
--
0
PMID: 17635639 TLR4 can also initiate a Mal/MyD88-independent signalling pathway through the recruitment of TRAM and TRIF.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c56 : 1
stoichiometry:c57 : 1
stoichiometry:c58 : 1
m28*m18998*0.1
nodelay
--
0
PMID: 17635639 TLR4 can also initiate a Mal/MyD88-independent signalling pathway through the recruitment of TRAM and TRIF.
p2
p2
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c4 : 1
stoichiometry:c6 : 1
stoichiometry:c5 : 1
m119368*m3965*0.1
nodelay
--
0
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.
p20
p20
cso30:i:ME_Binding
cso30:i:CC_Extracellular
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c59 : 1
stoichiometry:c60 : 1
stoichiometry:c61 : 1
stoichiometry:c62 : 1
m21*m30*m17258*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c63 : 1
stoichiometry:c64 : 1
m31*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c65 : 1
stoichiometry:c66 : 1
m32*0.1
nodelay
--
0
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.
p23
p23
cso30:i:ME_Phosphorylation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c67 : 1
stoichiometry:c69 : 1
stoichiometry:c68 : 1
m3973*m33*0.1
nodelay
--
0
PMID: 17635639 Active IRAK?1 also phosphorylates Tollip, supposedly a silencer for quiescent IRAK-1, which subsequently leaves the receptor complex
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c70 : 1
stoichiometry:c72 : 1
stoichiometry:c71 : 1
m34*0.1
nodelay
--
0
PMID: 17635639 Active IRAK?1 also phosphorylates Tollip, supposedly a silencer for quiescent IRAK-1, which subsequently leaves the receptor complex
p25
p25
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c73 : 1
stoichiometry:c74 : 1
stoichiometry:c75 : 1
stoichiometry:c76 : 1
m33*m36350*m183*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c77 : 1
stoichiometry:c78 : 1
stoichiometry:c79 : 1
m35*0.1
nodelay
--
0
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..
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c80 : 1
stoichiometry:c81 : 1
stoichiometry:c82 : 1
m38*m39*0.1
nodelay
--
0
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..
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c83 : 1
stoichiometry:c84 : 1
m40*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c85 : 1
stoichiometry:c86 : 1
stoichiometry:c87 : 1
m41*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c7 : 1
stoichiometry:c8 : 1
stoichiometry:c9 : 1
m2828*m155666*0.1
nodelay
--
0
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
p30
p30
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c130 : 1
stoichiometry:c89 : 1
m75*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c90 : 1
stoichiometry:c91 : 1
m43*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c92 : 1
stoichiometry:c93 : 1
m42*0.1
nodelay
--
0
PMID: 17635639 TIFA promotes the oligomerization and activation of TRAF6, leading to TRAF6 K63-linked polyubiquitination and subsequent TAK1 activation.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c94 : 1
stoichiometry:c95 : 1
m45*0.1
nodelay
--
0
PMID: 17635639 TIFA promotes the oligomerization and activation of TRAF6, leading to TRAF6 K63-linked polyubiquitination and subsequent TAK1 activation.
p34
p34
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c96 : 1
stoichiometry:c98 : 1
stoichiometry:c97 : 1
m47*m46*0.1
nodelay
--
0
PMID: 17635639, 11057907, 11460167 Active TAK1 then leads to the downstream activation of I¦ÊB kinases (IKK) and JNK or p38 MAPKs.
p35
p35
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c99 : 1
stoichiometry:c101 : 1
stoichiometry:c100 : 1
m49*m46*0.1
nodelay
--
0
PMID: 17635639, 11057907, 11460167 Active TAK1 then leads to the downstream activation of I¦ÊB kinases (IKK) and JNK or p38 MAPKs.
p36
p36
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c102 : 1
stoichiometry:c104 : 1
stoichiometry:c103 : 1
m64*m46*0.1
nodelay
--
0
PMID: 17635639, 11057907, 11460167 Active TAK1 then leads to the downstream activation of I¦ÊB kinases (IKK) and JNK or p38 MAPKs.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c105 : 1
stoichiometry:c107 : 1
stoichiometry:c106 : 1
m66*m48*0.1
nodelay
--
0
PMID: 17635639 IKKs eventually activate NF-¦ÊB by phosphorylating the NF-¦ÊB inhibitory protein I¦ÊB¦Á, 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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c108 : 1
stoichiometry:c110 : 1
stoichiometry:c109 : 1
m66*m63*0.1
nodelay
--
0
PMID: 17635639 IKKs eventually activate NF-¦ÊB by phosphorylating the NF-¦ÊB inhibitory protein I¦ÊB¦Á, 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.
p39
p39
cso30:i:ME_Phosphorylation
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c111 : 1
stoichiometry:c113 : 1
stoichiometry:c112 : 1
m67*m207*0.1
nodelay
--
0
PMID: 17635639 IKKs eventually activate NF-¦ÊB by phosphorylating the NF-¦ÊB inhibitory protein I¦ÊB¦Á, 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
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c10 : 1
stoichiometry:c11 : 1
stoichiometry:c12 : 1
m3966*m6485*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c114 : 1
stoichiometry:c115 : 1
m68*0.1
nodelay
--
0
PMID: 17635639 IKKs eventually activate NF-¦ÊB by phosphorylating the NF-¦ÊB inhibitory protein I¦ÊB¦Á, 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
p41
p41
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c116 : 1
stoichiometry:c117 : 1
stoichiometry:c118 : 1
m69*0.1
nodelay
--
0
PMID: 17635639 IKKs eventually activate NF-¦ÊB by phosphorylating the NF-¦ÊB inhibitory protein I¦ÊB¦Á, 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
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c119 : 1
stoichiometry:c120 : 1
stoichiometry:c131 : 1
m71*m174*0.1
nodelay
--
0
PMID: 17635639, 12874243 Pellino-3 was also shown to bind the Ser/Thr kinase NIK.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c121 : 1
stoichiometry:c122 : 1
stoichiometry:c123 : 1
m19288*m40*0.1
nodelay
--
0
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-¦ÊB and MAPKs.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c124 : 1
stoichiometry:c125 : 1
m72*0.1
nodelay
--
0
PMID: 17635639 Pellino proteins associate with IRAK-1, TRAF6 and TAK1 and become phosphorylated by IRAK-1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c126 : 1
stoichiometry:c127 : 1
stoichiometry:c128 : 1
m19288*m42*0.1
nodelay
--
0
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-¦ÊB and MAPKs.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c88 : 1
stoichiometry:c129 : 1
m73*0.1
nodelay
--
0
PMID: 17635639 Pellino-1 and -2 also induce IRAK-1 polyubiquitination.
p47
p47
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c132 : 1
stoichiometry:c133 : 1
stoichiometry:c141 : 1
stoichiometry:c134 : 1
m19287*m2522*m79*0.1
nodelay
--
0
PMID: 17635639, 16951688 Pellino-1 was recently found to interact with Smad6, an anti-inflammatory protein induced by TGF-¦Â.
p48
p48
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c135 : 1
stoichiometry:c136 : 1
stoichiometry:c137 : 1
stoichiometry:c139 : 1
stoichiometry:c140 : 1
stoichiometry:c138 : 1
m19287*m30*m183*m185*0.1
nodelay
--
0
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.
p49
p49
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c142 : 1
stoichiometry:c143 : 1
stoichiometry:c144 : 1
m19287*m1572*0.1
nodelay
--
0
PMID: 17635639, 16951688 the same group also reported an interaction between Pellino-1 and the TLR/IL-1R adaptor protein MyD88.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c13 : 1
stoichiometry:c14 : 1
stoichiometry:c15 : 1
m14*m19940*0.1
nodelay
--
0
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.
p50
p50
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c145 : 1
stoichiometry:c146 : 1
stoichiometry:c147 : 1
m19301*m21910*0.1
nodelay
--
0
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.
p51
p51
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c148 : 1
stoichiometry:c150 : 1
stoichiometry:c149 : 1
m47*m71*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
p52
p52
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c151 : 1
stoichiometry:c153 : 1
stoichiometry:c152 : 1
m49*m71*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
p53
p53
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c154 : 1
stoichiometry:c156 : 1
stoichiometry:c155 : 1
m82*m71*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
p54
p54
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c157 : 1
stoichiometry:c163 : 1
stoichiometry:c158 : 1
m84*m83*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
p55
p55
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c159 : 1
stoichiometry:c164 : 1
stoichiometry:c160 : 1
m84*m48*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
p56
p56
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c161 : 1
stoichiometry:c165 : 1
stoichiometry:c162 : 1
m84*m63*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
p57
p57
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c166 : 1
stoichiometry:c172 : 1
stoichiometry:c167 : 1
m87*m48*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
p58
p58
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c168 : 1
stoichiometry:c173 : 1
stoichiometry:c169 : 1
m87*m83*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
p59
p59
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c170 : 1
stoichiometry:c174 : 1
stoichiometry:c171 : 1
m87*m63*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c16 : 1
stoichiometry:c17 : 1
stoichiometry:c18 : 1
m14*m19823*0.1
nodelay
--
0
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.
p60
p60
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c175 : 1
stoichiometry:c183 : 1
stoichiometry:c176 : 1
m2057*m63*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
p61
p61
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c177 : 1
stoichiometry:c182 : 1
stoichiometry:c178 : 1
m2057*m83*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
p62
p62
cso30:i:ME_UnknownActivation
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c179 : 1
stoichiometry:c181 : 1
stoichiometry:c180 : 1
m2057*m48*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c184 : 1
stoichiometry:c192 : 1
stoichiometry:c185 : 1
m89*m83*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c186 : 1
stoichiometry:c191 : 1
stoichiometry:c187 : 1
m89*m63*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c188 : 1
stoichiometry:c190 : 1
stoichiometry:c189 : 1
m89*m48*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c193 : 1
stoichiometry:c194 : 1
m90*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c196 : 1
stoichiometry:c195 : 1
m88*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
p68
p68
cso30:i:ME_GeneExpression
cso30:i:CC_Nucleoplasm
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c197 : 1
stoichiometry:c198 : 1
m86*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c200 : 1
stoichiometry:c199 : 1
m85*0.1
nodelay
--
0
PMID: 17635639, 12874243, 15917247 Overexpression of Pellino-3 has no effect on NF-¦ÊB activation, but activates ERK, JNK and p38 MAPKs, leading to the activation of Elk-1, c-Jun, CREB and CHOP dependent gene expression
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c19 : 1
stoichiometry:c20 : 1
stoichiometry:c21 : 1
m19828*m16*0.1
nodelay
--
0
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c201 : 1
stoichiometry:c202 : 1
stoichiometry:c203 : 1
m71*m30*0.1
nodelay
--
0
PMID: 17635639, 15917247, 16884718, 12496252, 12370331, 12860405, 16951688, 15917247 all mammalian Pellino proteins were shown to interact with IRAK-1 and IRAK-4.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c204 : 1
stoichiometry:c205 : 1
stoichiometry:c206 : 1
m19301*m30*0.1
nodelay
--
0
PMID: 17635639, 15917247, 16884718, 12496252, 12370331, 12860405, 16951688, 15917247 all mammalian Pellino proteins were shown to interact with IRAK-1 and IRAK-4.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c207 : 1
stoichiometry:c208 : 1
m19287*m30*0.1
nodelay
--
0
PMID: 17635639, 15917247, 16884718, 12496252, 12370331, 12860405, 16951688, 15917247 all mammalian Pellino proteins were shown to interact with IRAK-1 and IRAK-4.
p73
p73
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c209 : 1
stoichiometry:c211 : 1
stoichiometry:c210 : 1
m19287*m17258*0.1
nodelay
--
0
PMID: 17635639, 15917247, 16884718, 12496252, 12370331, 12860405, 16951688, 15917247 all mammalian Pellino proteins were shown to interact with IRAK-1 and IRAK-4.
p74
p74
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c212 : 1
stoichiometry:c214 : 1
stoichiometry:c213 : 1
m19301*m17258*0.1
nodelay
--
0
PMID: 17635639, 15917247, 16884718, 12496252, 12370331, 12860405, 16951688, 15917247 all mammalian Pellino proteins were shown to interact with IRAK-1 and IRAK-4.
p75
p75
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c215 : 1
stoichiometry:c216 : 1
stoichiometry:c217 : 1
m19301*m183*0.1
nodelay
--
0
PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1.
p76
p76
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c218 : 1
stoichiometry:c219 : 1
stoichiometry:c220 : 1
m19287*m183*0.1
nodelay
--
0
PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c221 : 1
stoichiometry:c222 : 1
stoichiometry:c223 : 1
m71*m183*0.1
nodelay
--
0
PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1.
p79
p79
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c224 : 1
stoichiometry:c225 : 1
stoichiometry:c226 : 1
m1573*m19287*0.1
nodelay
--
0
PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c22 : 1
stoichiometry:c23 : 1
stoichiometry:c24 : 1
m3961*m6438*0.1
nodelay
--
0
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
p80
p80
cso30:i:ME_Binding
cso30:i:CC_Cytosol
--
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c227 : 1
stoichiometry:c228 : 1
stoichiometry:c229 : 1
m1573*m19301*0.1
nodelay
--
0
PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c230 : 1
stoichiometry:c231 : 1
stoichiometry:c232 : 1
m1573*m71*0.1
nodelay
--
0
PMID: 17635639, 12874243, 12496252, 16951688, 15917247, 12804775 all three mammalian Pellino proteins also interact with TRAF6 and TAK1.
p82
p82
cso30:i:ME_ProteasomeDegradation
cso30:i:CC_Extracellular
--
--
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.
--
and
mass
coefficient1:0.1
coefficient2:1.0
stoichiometry:c25 : 1
stoichiometry:c26 : 1
stoichiometry:c27 : 1
stoichiometry:c28 : 1
m19*m18*0.1
nodelay
--
0
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
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputInhibitor
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputProcess
threshold
--
0
1,
--
cso30:c:OutputProcess
threshold
--
0
1,
--
cso30:c:InputAssociation
threshold
--
0
1,
--