Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.99957355 |
Here we show that TRADD directly interacts with TRAF 2 and FADD , signal transducers that activate NF kappa B and induce apoptosis , respectively . 0.99957355^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
DR 3 signal transduction is mediated by a complex of intracellular signaling molecules including TRADD , TRAF 2 , FADD , and FLICE . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
The recruitment of TRAF 2 and c IAP 1 to TNF R 1 is TNF dependent , is mediated by TRADD , and is independent of TNF R 2 . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Hepatitis C virus core protein potentiates c Jun N terminal kinase activation through a signaling complex involving TRADD and TRAF 2 . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
The data suggest that entry of TRAF 6 into the LMP 1 complex is mediated by TRADD and TRAF 2 . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Isolation and characterization of death domain ( TNF RI , Fas , TRADD , FADD / MORT 1 , RIP ) and TRAF domain containing proteins ( TRAF 1 , TRAF 2 , TRAF 3 ) have partially bridged a large molecular gap within one of several signaling pathways which originate at the plasma membrane and terminate in the nucleus . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Interaction of TRAF 2 with TNF R 2 and TRADD requires sequences at the C terminus of the TRAF C domain , whereas interaction with the protein kinase receptor interacting protein 5 ( RIP ) occurs via sequences at the N terminus of the TRAF C domain . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
TRAF 2 , a cytoplasmic protein that binds to the p 75 TNF receptor , as well as to several other receptors of the TNF / NGF family , also binds to TRADD , thus further extending the range of receptors of this family that can share common signaling mechanisms . ^^^ |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Interaction of the p 55 tumor necrosis factor receptor 1 ( TNF R 1 ) associated signal transducer TRADD with FADD signals apoptosis , whereas the TNF receptor associated factor 2 protein ( TRAF 2 ) is required for activation of the nuclear transcription factor nuclear factor kappa B . ^^^ |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
One site is similar to activated TNFRII in associating with TNFR associated factors TRAF 1 and TRAF 2 , and the second site is similar to TNFRI in associating with the TNFRI death domain interacting protein TRADD . ^^^ TNFRI has been recently shown to activate NF kappaB through association with TRADD , RIP , and TRAF 2 ; activation of the NF kappaB inducing kinase ( NIK ) ; activation of the IkappaB alpha kinases ( IKKalpha and IKKbeta ) ; and phosphorylation of IkappaB alpha . ^^^ |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
TNF alpha signaling involves the recruitment of at least three proteins ( TRADD , RIP , and TRAF 2 ) to the type 1 TNF alpha receptor tail , leading to the sequential activation of the downstream NF kappaB inducing kinase ( NIK ) and IkappaB specific kinases ( IKKalpha and IKKbeta ) . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Epstein Barr virus encoded latent membrane protein 1 activates the JNK pathway through its extreme C terminus via a mechanism involving TRADD and TRAF 2 . ^^^ The ability of CTAR 1 to activate NF kappaB appears to be attributable to the direct interaction of tumor necrosis factor ( TNF ) receptor associated factor 2 ( TRAF 2 ) , while recent work indicates that CTAR 2 induced NF kappaB is mediated through its association with TNF receptor associated death domain ( TRADD ) . ^^^ TRAF 2 is known to associate with TRADD , and expression of a dominant negative N terminal deletion TRAF 2 mutant was found to partially inhibit LMP 1 induced JNK activation in 293 cells . ^^^ These data further define a role for TRADD and TRAF 2 in JNK activation and confirm that LMP 1 utilizes signalling mechanisms used by the TNF receptor / CD40 family to elicit its pleiotropic activities . . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
TNF treatment released SODD from TNF R 1 , permitting the recruitment of proteins such as TRADD and TRAF 2 to the active TNF R 1 signaling complex . ^^^ |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
The constitutive expression of TNF receptors ( TNFRI and TNFRII ) and the adapter molecules , including TNFR associated death domain protein ( TRADD ) , TNFR associated factor 2 ( TRAF 2 ) , and receptor interacting protein ( RIP ) , were analyzed both at the protein level by flow cytometry or Western blotting , and at the mRNA level using quantitative PCR or Northern blotting in lymphocytes from aged and young subjects . ^^^ An increased constitutive expression of TNFRI and TRADD and decreased expression of TNFRII and TRAF 2 were observed in lymphocytes from aged as compared with young controls . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
No changes in the levels or molecular weights of the adaptor proteins TRADD ( TNF receptor associated death domain ) , RIP ( receptor interacting protein ) , or TRAF 2 ( TNF receptor associated factor 2 ) were caused by apoptogenic drugs . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
LMP 1 signal transduction differs substantially from TNF receptor 1 signaling in the molecular functions of TRADD and TRAF 2 . ^^^ Whereas NF kappaB activation by LMP 1 was blocked by a dominant negative TRADD mutant , LMP 1 induces JNK 1 independently of the TRADD death domain and TRAF 2 , which binds to TRADD . ^^^ Although both LMP 1 and TNFR 1 interact with TRADD and TRAF 2 , the different topologies of the signaling complexes correlate with substantial differences between LMP 1 and TNFR 1 signal transduction to JNK1 . . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Moreover , NF kappaB activation induced by overexpression of the TNF receptor associated proteins TNF receptor associated death domain protein ( TRADD ) , receptor interacting protein ( RIP ) , and TNF recep tor associated factor 2 ( TRAF 2 ) was also inhibited by expression of A 20 , whereas NF kappaB activation induced by overexpression of NF kappaB inducing kinase ( NIK ) or the human T cell leukemia virus type 1 ( HTLV 1 ) Tax was unaffected . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
LMP 1 spontaneously aggregates in the plasma membrane and enables two transformation effector sites ( TES 1 and TES 2 ) within the 200 amino acid cytoplasmic carboxyl terminus to constitutively engage the tumor necrosis factor receptor ( TNFR ) associated factors TRAF 1 , TRAF 2 , TRAF 3 , and TRAF 5 and the TNFR associated death domain proteins TRADD and RIP , thereby activating NF kappaB and c Jun N terminal kinase ( JNK ) . ^^^ Mutant and wt LMP 1 proteins were also similar in their constitutive association with TRAF 1 , TRAF 2 , TRAF 3 , TRADD , and RIP . ^^^ |
|
Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Examination of Stat 1 deficient cells showed an apparent increase in TNF alpha induced TRADD RIP and TRADD TRAF 2 complex formation , while interaction between TRADD and FADD was unaffected . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD TRAF 2 interaction . ^^^ We now report the structure of the TRADD TRAF 2 complex , which is highly distinct from receptor TRAF 2 interactions . ^^^ This interaction is significantly stronger and we show by an in vivo signaling assay that TRAF 2 signaling is more readily initiated by TRADD than by direct receptor TRAF 2 interactions . ^^^ TRADD is specific for TRAF 1 and TRAF 2 , which ensures the recruitment of clAPs for the direct inhibition of caspase activation in the signaling complex . ^^^ The stronger affinity and unique specificity of the TRADD TRAF 2 interaction are crucial for the suppression of apoptosis and provide a mechanistic basis for the perturbation of TRAF recruitment in sensitizing cell death induction . . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Solution structure of N TRADD and characterization of the interaction of N TRADD and C TRAF 2 , a key step in the TNFR 1 signaling pathway . ^^^ The N terminal domain ( N TRADD ) promotes the recruitment of TRAF 2 to TNFR 1 by binding to the C terminal of TRAF 2 , leading to the activation of JNK / AP1 and NF kappa B . ^^^ A combination of NMR , BIAcore , and mutagenesis experiments was used to help identify the site of interaction of N TRADD with C TRAF 2 , providing a framework for future attempts to selectively inhibit the TNF signaling pathways . . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Upon TNF treatment , the TRAF 2 caveolin 1 complex transiently associates with TRADD , and upon overexpression of TNFR 2 , the TRAF 2 caveolin 1 complex stably associates with and causes redistribution of this receptor as detected by confocal fluorescence microscopy . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
The expression of adapter molecules TNF receptor associated death domain ( TRADD ) , Fas associated death domain ( FADD ) and TNF associated factor 2 ( TRAF 2 ) and caspase 3 was analyzed by Western blotting . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
In this study , we further examined the interaction of the core protein with the signaling molecules of TNFR 1 , including FADD , TRADD , and TRAF 2 , in a human embryonic kidney cell line , HEK 293 , that overexpresses the HCV core protein . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
The critical role of TRAF 1 in the regulation of TRAF 2 dependent JNK signaling is particular to the TRAF binding domain of LMP 1 , since a homologous region in the cytoplasmic tail of CD 40 or the TRADD interacting domain of LMP 1 signal on the JNK axis independently of TRAF 1 status . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
The constitutive expression of mRNA for TNF receptors ( TNFR ) , including TNFRI and TNFRII , and the adapter molecules , such as the TNF receptor associated death domain protein ( TRADD ) , Fas associated death domain protein ( FADD ) , receptor interacting protein ( RIP ) and TNF receptor associated factor 2 ( TRAF 2 ) were analyzed by reverse transcriptase ( RT ) PCR in bone marrow samples from control , MDS and AML cases . ^^^ An increased constitutive expression of mRNA for TRADD , FADD and RIP and decreased expression of mRNA for TRAF 2 were observed in bone marrow cells from MDS patients , especially from RA patients , as compared with controls , although the differences were not significant . ^^^ These data suggested enhanced signaling by the TNFRI TRADD FADD pathway and suppressed signaling by the TRAF 2 pathway in RA . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
TRADD also binds two other adaptors receptor interacting protein ( RIP ) and TNF receptor associated factor 2 ( TRAF 2 ) , which are required for TNF induced NF kappaB and c Jun N terminal kinase activation , respectively . ^^^ Analysis of the native TNF signaling complex revealed the recruitment of RIP , TRADD , and TRAF 2 but not FADD or caspase 8 . ^^^ In an in vitro binding assay , the intracellular domain of TNF R 1 bound TRADD , RIP , and TRAF 2 but did not bind FADD or caspase 8 . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Here we show that upon TNFalpha binding , TNFR 1 translocates to cholesterol and sphingolipid enriched membrane microdomains , termed lipid rafts , where it associates with the Ser / Thr kinase RIP and the adaptor proteins TRADD and TRAF 2 , forming a signaling complex . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
TL1A induced the formation of a DR 3 signaling complex containing TRADD , TRAF 2 , and RIP and activated the NF kappaB and the ERK , JNK , and p 38 mitogen activated protein kinase pathways . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
The initial plasma membrane bound complex ( complex 1 ) consists of TNFR 1 , the adaptor TRADD , the kinase RIP 1 , and TRAF 2 and rapidly signals activation of NF kappa B . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Immunoprecipitation of TNF R 1 revealed that in response to H2O2 , the adapter proteins , TRADD and TRAF 2 , and JNK were recruited to the receptor . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
The first complex ( complex 1 ) is formed at the membrane by TNF R 1 , TRADD , RIP , TRAF 2 and c IAP 1 , while the second complex ( complex 2 ) , formed in the cytosol , predominantly contains FADD and pro caspases 8 / 10 but lacks TNF R 1 . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Overexpression of TRAF 1 , however , had no effect on the interaction of TRADD and TRAF 2 , known to be important for tumor necrosis factor receptor 1 ( TNF R 1 ) mediated NF kappaB activation . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Co precipitation and co immunoprecipitation assays revealed that TRUSS can interact with TRADD , TRAF 2 , and components of the IKK complex . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Its dominant negative effects were due to binding and sequestration of LMP 1 adapters TRAF 2 and TRADD as assessed by coimmunoprecipitation experiments and confocal analysis . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
SCH 66336 also inhibited the NF kappaB dependent reporter gene expression activated by TNF , TNFR 1 , TRADD , TRAF 2 , NIK , and IKK but not that activated by the p 65 subunit of NF kappaB . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
An important regulatory step in control of antiapoptotic signaling is the assembly of the TNFR 1 TNFR 1 associated death domain protein ( TRADD ) TNFR associated factor 2 ( TRAF 2 ) receptor interacting protein ( RIP ) complex that controls NF kappaB activation . ^^^ These results suggest that delta PKC and PI 3 kinase regulate TNF antiapoptotic signaling at the level of the TNFR 1 through control of assembly of a TNFR 1 TRADD RIP TRAF 2 complex . . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
TNAP specifically inhibits NF kappaB activation induced by tumor necrosis factor ( TNF ) alpha , TNF receptor 1 , TRADD , RIP , TRAF 2 , and NIK but does not affect IKK 1 and IKK 2 mediated NF kappaB activation . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
TNF binding induces release of AIP 1 from TNFR 1 , resulting in cytoplasmic translocation and concomitant formation of an intracellular signaling complex comprised of TRADD , RIP 1 , TRAF 2 , and AIPl . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NF kappaB dependent reporter gene transcription induced by TNF , TNFR 1 , TRADD , TRAF 2 , NIK , and IKK was also blocked by guggulsterone but without affecting p 65 mediated gene transcription . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Seven proteins were identified , including TRADD , TRAP 2 , and TRAF 2 , which are three proteins known to be recruited to TNFalpha receptors . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
In the normal rat cortex , a portion of TNFR 1 was present in lipid raft microdomains , where it associated with the adaptor proteins TRADD ( TNF receptor associated death domain ) , TNF receptor associated factor 2 ( TRAF 2 ) , the Ser / Thr kinase RIP ( receptor interacting protein ) , TRAF 1 , and cIAP 1 ( cellular inhibitor of apoptosis protein 1 ) , forming a survival signaling complex . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
IL 8 induced NF kappaB activation is for the most part unaltered when cells are transfected with dominant negative TRADD , FADD , or TRAF 2 , but is inhibited with dominant negative TRAF 6 , NIK , IKK , or IkappaBalpha transfected cells . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Evodiamine also inhibited the NF kappaB dependent reporter gene expression activated by TNF , TNFR 1 , TRADD , TRAF 2 , NIK , and IKK but not that activated by the p 65 subunit of NF kappaB . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Zerumbone also inhibited the NF kappaB dependent reporter gene expression activated by TNF , TNFR 1 , TRADD , TRAF 2 , NIK , and IKK but not that activated by the p 65 subunit of NF kappaB . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
The analysed factors included TNF alpha , TNFR 1 , TNF receptor associated death domain ( TRADD ) , caspase 3 , caspase 8 , TNF receptor associated factor 2 ( TRAF 2 ) and receptor interactive protein ( RIP ) , all of which are involved in the TNF alpha / TNFR 1 signalling pathway mediated apoptosis . ^^^ The quantitative RT PCR indicated that the infected muscle tissues up regulate the expression of pro apoptosis genes ( TNF alpha , TNFR 1 and TRADD , caspase 3 and caspase 8 ) , and anti apoptosis genes ( TRAF 2 and RIP ) at the beginning of cyst formation . ^^^ The in situ localization study of proapoptosis ( TRADD , caspase 3 ) and anti apoptosis gene products ( TRAF 2 ) indicated that these were expressed in the basophilic cytoplasm ( infected muscle cell origin ) of the nurse cells . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
NF kappaB dependent reporter gene expression was also suppressed by 4 HPR , as was NF kappaB reporter activity induced by TNFR 1 , TRADD , TRAF 2 , NIK , and IKK but not that induced by p 65 transfection . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
Furthermore , SAHA inhibited the NF kappaB dependent reporter gene expression activated by TNF , TNFR 1 , TRADD , TRAF 2 , NF kappaB inducing kinase , IkappaBalpha kinase , and the p 65 subunit of NF kappaB . ^^^ |
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Interacting proteins: Q15628 and Q12933 |
Pubmed |
SVM Score :0.0 |
The constitutive expression of mRNA for TNF alpha receptors ( TNFR 1 and TNFR 2 ) and the adapter molecules , such as the TNF receptor associated death domain protein ( TRADD ) , Fas associated death domain protein ( FADD ) , receptor interacting protein ( RIP ) , and TNF receptor associated factor 2 ( TRAF 2 ) were analyzed by reverse transcriptase PCR ( RT PCR ) in PBMCs from control and RA cases . ^^^ PBMCs of RA patients showed a significant increase in TNF alpha and TNFR 1 expression as compared with that from control subjects along with significantly increased constitutive expression of TRADD , RIP , and TRAF 2 mRNA . ^^^ These data suggested enhanced signaling by the TNFR 1 TRADD RIP TRAF 2 pathway and suppressed signaling by the TNFR 1 TRADD FADD pathway in PBMCs of RA patients . ^^^ |
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