| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.66171607 |
| TRADD reverses these roles , employing a Pelle like surface to interact with either receptor TNFR 1 or adaptor FADD . 0.66171607^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.76943923 |
| The death domain of tumor necrosis factor ( TNF ) receptor 1 ( TNFR 1 ) triggers distinct signaling pathways leading to apoptosis and NF kappa B activation through its interaction with the death domain protein TRADD . 0.76943923^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.59572035 |
| The association of TRADD , a 34 kDa cytoplasmic protein containing a C terminal death domain , with aggregated TNF receptor 1 ( TNF R 1 ) through their respective death domains leads to NF kappa B activation and programmed cell death . 0.59572035^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.83702059 |
| 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 . 0.83702059^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.80751808 |
| The C terminal fragment of RIP also enhanced the association between TNFR 1 and death domain proteins including TNFR 1 associated death domain ( TRADD ) and Fas associated death domain ( FADD ) , resulting in the activation of caspase 8 and stimulation of apoptosis . 0.80751808^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.92543122 |
| These results indicate that K 18 may sequester TRADD to attenuate interactions between TRADD and activated TNFR 1 and moderate TNF induced apoptosis in simple epithelial cells . . 0.92543122^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| A TNF R 1 associated protein TRADD has been discovered that interacts with the death domain of the receptor . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Upon activation of these receptors , Fas / APO 1 binds a protein called MORT 1 ( or FADD ) and p 55 R binds a protein called TRADD . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| WSL 1 also interacts specifically with the TNFR 1 associated molecule TRADD . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| DR 6 interacts with TRADD , which has previously been shown to associate with TNFR 1 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Furthermore , TNF dependent recruitment of TRADD to surface TNFR 1 was also inhibited . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| We found that actinomycin D treatment of KS cells selectively abolished expression of mitogen activated protein kinase activating death domain protein ( MADD ) , a novel TNFR 1 associated death domain protein . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Using the ribonuclease ( RNase ) protection assay and the reverse transcriptase polymerase chain reaction ( RT PCR ) method , we confirmed that TNF receptor 1 ( TNFR 1 ) , TNFR 1 associated death domain protein ( TRADD ) , Fas receptor associated intracellular protein with death domain ( FADD ) , and FADD like interleukin 1beta converting enzyme ( FLICE ) were expressed in the pancreatic beta cell line , MIN 6 cells . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Activated tumor necrosis factor alpha ( TNF alpha ) receptor 1 ( TNFR 1 ) recruits TNFR 1 associated death domain protein ( TRADD ) , which in turn triggers two opposite signaling pathways leading to caspase activation for apoptosis induction and NF kappaB activation for antiapoptosis gene upregulation . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| TNFR 1 associated death domain protein ( TRADD ) contains an N terminal TRAF binding domain and a C terminal death domain along with nuclear import and export sequences that cause shuttling between the cytoplasm and nucleus . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| In vivo protein protein interaction studies displayed an association between TNF receptor 1 ( TNFR 1 ) and TNFR 1 associated death domain protein ( TRADD ) , suggesting that the core protein does not perturb this interaction . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Analysis of the upstream signaling events affected by PMA revealed that it markedly inhibited the TNF induced recruitment of TNFR 1 associated death domain protein ( TRADD ) and receptor interacting protein ( RIP ) to TNFR 1 , subsequently inhibiting TNF induced activation of nuclear factor kappaB and c Jun NH 2 terminal kinase ( JNK ) . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| We have identified a novel 34 kDa protein , designated TRADD , that specifically interacts with an intracellular domain of TNFR 1 known to be essential for mediating programmed cell death . ^^^ The C terminal 118 amino acids of TRADD are sufficient to trigger both of these activities and likewise sufficient for interaction with the death domain of TNFR 1 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| TRADD is a TNFR 1 associated signal transducer that is involved in activating both pathways . ^^^ Thus , these two TNFR 1 TRADD signaling cascades appear to bifurcate at TRADD . . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| One , MORT 1 ( also called FADD ) , binds to Fas / APO1 but not to p 55 R ; another , TRADD , binds to the p 55 TNF receptor but not to Fas / APO1 ; and the third , RIP , binds weakly to both receptors . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Furthermore , a molecule called TRADD has been identified that associates with the cytoplasmic segment of TNFR 1 . ^^^ TRADD , which contains a novel ' death domain ' that binds to the corresponding death domain in the cytoplasmic segment of TNFR 1 , can mediate both activation of NF kappa B and induction of apoptosis , the two major responses signaled by TNFR1 . . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| The human TNF R 1 associated death domain protein ( TRADD ) induces cell death and NF kappa B activation when overexpressed . ^^^ Mouse TRADD specifically interacts with wild type TNF R 1 but not with a truncated mutant TNF R 1 lacking its C terminal 20 amino acids . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 P19438 |
Pubmed |
SVM Score :0.0 |
| The flow of death signals from TNFR 1 occurs through the adaptor molecule tumor necrosis factor receptor associated death domain protein ( TRADD ) to FADD to FLICE , whereas for CD 95 the receptor directly communicates with FADD and then FLICE . ^^^ MC 159 and E 8 inhibited both TNFR 1 and CD 95 induced apoptosis as well as killing mediated by overexpression of the downstream adaptors TRADD and FADD . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| The adapter protein TRADD binds to TNF R 55 in a ligand dependent manner and serves as anchor for the subsequent recruitment of other proteins into the signaling complex that directly lead to cell death or nuclear factor kappaB ( NF kappaB ) induction . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| TNFR 1 recruits and assembles a signaling complex containing a number of death domain ( DD ) containing proteins , including the adaptor protein TRADD and the serine / threonine kinase RIP , which mediates TNF induced NF kappa B activation . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 P19438 |
Pubmed |
SVM Score :0.0 |
| TNF recruits TRADD to the plasma membrane but not the trans Golgi network , the principal subcellular location of TNF R 1 . ^^^ The subcellular interactions of TNF R 1 and the TRADD ( TNFR associated death domain protein ) adaptor protein have been analyzed in the human monocyte cell line U 937 and the human endothelial cell line ECV 304 by confocal immunofluorescence microscopy and by Western blot analysis of fractionated cell extracts . ^^^ In untreated cells , in which TNF R 1 is found on the cell surface but principally localizes to the trans Golgi network , TRADD is concentrated in the cis or medial Golgi region , but separates from the Golgi during cell fractionation . ^^^ Coimmunoprecipitation studies have shown that TRADD binds to TNF R 1 within 1 min of TNF treatment in a cell fraction containing plasma membrane . ^^^ In contrast , no association is detected between TRADD and TNF R 1 in the Golgi in response to exogenous TNF at any time examined . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| In contrast to TNFR 1 , LMP 1 recruits TRADD via the TRADD N terminus but not the TRADD death domain . ^^^ Consequently , the molecular function of TRADD in LMP 1 signaling differs from its role in TNFR 1 signal transduction . ^^^ 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 . . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| The tumor necrosis factor receptor 1 ( TNFR 1 ) and the Fas receptor recruit complexes formed by the interactions between RIP kinase , TRADD , FADD and RAIDD adaptor proteins that contain death domains which in turn recruit other proteins to initiate signaling [ 1 ] [ 2 ] [ 3 ] [ 4 ] [ 5 ] . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| A site in the Epstein Barr virus ( EBV ) transforming protein LMP 1 that constitutively associates with the tumor necrosis factor receptor 1 ( TNFR 1 ) associated death domain protein TRADD to mediate NF kappaB and c Jun N terminal kinase activation is critical for long term lymphoblastoid cell proliferation . ^^^ We now find that LMP 1 signaling through TRADD differs from TNFR 1 signaling through TRADD . ^^^ LMP 1 needs only 11 amino acids to activate NF kappaB or synergize with TRADD in NF kappaB activation , while TNFR 1 requires approximately 70 residues . ^^^ Further , LMP 1 does not require TRADD residues 294 to 312 for NF kappaB activation , while TNFR 1 requires TRADD residues 296 to 302 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| A mutant of Casper and the caspase specific inhibitors crmA and BD fmk partially inhibit TNF R 1 , TRADD , and TNF induced NF kappaB activation , suggesting that FADD , Casper , and caspase 8 function downstream of TRADD and contribute to TNF R 1 induced NF kappaB activation . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Transcriptional expression of TNFR 1 ( p 55 ) , as well as that of FLICE , Fas , FADD , DR 3 , FAF , TRADD , and RIP was similar in these cell lines , indicating that the susceptibility to TNFalpha induced apoptosis may not be determined by the constitutive expression level of these factors . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Fas binds FADD directly , whereas TNFR 1 binds FADD indirectly , through TRADD . ^^^ TRADD and RIP , which bound TNFR 1 , did not bind DR 4 and DR 5 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| These results provide important insight into the molecular interactions mediating TNFR DD self association and subsequent recruitment of TRADD in the signaling activity of TNFR 1 . . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ TRADD is a multifunctional signaling adaptor protein that is recruited to TNFR 1 upon ligand binding . ^^^ The C terminal of TRADD comprises the `` death domain ' ' that is responsible for association of TNFR 1 and other death domain containing proteins such as FADD and RIP . ^^^ 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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| FADD DD provides the site of FADD recruitment to death receptor complexes at the plasma membrane by , for example , interaction with the Fas receptor cytoplasmic death domain ( Fas DD ) , or binding of the TNF R 1 adapter molecule TRADD . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| These families may include receptor / ligand molecules such as Fas , Fas ligand , tumor necrosis factor receptor 1 ( TNFR 1 ) , and TNF related apoptosis inducing ligand ( TRAIL ) ; signal transduction adapter molecules such as Fas associated death domain ( FADD ) , TNFR 1 associated death domain ( TRADD ) , receptor interacting protein ( RIP ) , Fas associated factor ( FAF ) , and Fas associated phosphatase ( FAP ) ; or effector molecules such as caspases . ^^^ To detect the expression of apoptosis related molecules , ribonuclease protection assay was used with specific antisense RNA probes for Fas , Fas ligand , TNFR 1 , TRAIL , FADD , TRADD , RIP , FAF , FAP , and caspase 8 . ^^^ Compared with control and contralateral kidneys , the ligated kidneys displayed a dynamic expression of mRNAs for many apoptosis related molecules , which included an up to threefold increase for Fas , Fas ligand , TNF R 1 , TRAIL , TRADD , RIP , and caspase 8 , and an up to twofold increase for FADD and FAP , but there was little change for FAF . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| The serine / threonine kinase HIPK 2 interacts with TRADD , but not with CD 95 or TNF R 1 in 293T cells . ^^^ Here we describe that HIPK 2 can also associate with TRADD , a protein that interacts with tumor necrosis factor receptor type 1 ( TNF R 1 ) . ^^^ Under the conditions where HIPK2 / TRADD association was found , no direct interaction of HIPK 2 with CD 95 , TNF R 1 , FADD or caspase 8 could be detected . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Treatment with 10 ( 7 ) M ICI or 10 ( 7 ) M Tam leads to a time dependent increase of TNFR 1 and TRADD steady state mRNA levels in MCF 7 cells . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Tumor necrosis factor ( TNF ) receptor associated factor ( TRAF ) 2 is an intracellular adapter protein , which , upon TNF stimulation , is directly recruited to the intracellular region of TNF receptor 2 ( TNFR 2 ) or indirectly , via TRADD , to the intracellular region of TNF receptor 1 ( TNFR 1 ) . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Furthermore , expression of TNFR 1 , TRADD and caspase 3 was decreased in cord blood lymphocytes as compared to peripheral blood lymphocytes . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Furthermore , we demonstrate that HCV core protein does not compete with TNF receptor associated death domain ( TRADD ) for its interaction with the death domain of TNFR 1 . ^^^ Our in vivo data show that HCV core and TRADD form a ternary complex with TNFR 1 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ In contrast , the core protein did not directly interact with the DD of TRADD , but could disrupt the binding of TRADD to TNFR 1 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| In these structures , the TRADD death domain ( TRADD DD ) can activate an apoptosis pathway that is mechanistically distinct from its action at the membrane bound TNFR 1 complex . ^^^ The adapter protein tumor necrosis factor receptor ( TNFR ) 1 associated death domain ( TRADD ) plays an essential role in recruiting signaling molecules to the TNFRI receptor complex at the cell membrane . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| These data suggest that despite some similarity between the death domains of TR 3 and TNFR 1 the nature of the interaction with TRADD differs from that reported for TNFR1 . . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| AD cases had increased levels of proapoptotic markers including tumor necrosis factor alpha ( TNFalpha ) , TNF receptor type 1 ( TNF R 1 ) , TNF receptor associated death domain ( TRADD ) , and caspase 3 , 2 to 10 fold higher ( P < . 01 ) than age matched controls and 1 to 3 times higher than transitional cases . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ These data suggested enhanced signaling by the TNFRI TRADD FADD pathway and suppressed signaling by the TRAF 2 pathway in RA . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| CD 95 , TNF related apoptosis inducing ligand ( TRAIL R 1 ) , and TRAIL R 2 bind FADD directly , whereas recruitment to TNF R 1 is indirect through another adaptor TNF receptor associated death domain protein ( TRADD ) . ^^^ 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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| LMP 1 associates simultaneously with lipid rafts and with its signaling molecules , tumor necrosis factor receptor ( TNF R ) associated factors ( TRAFs ) and TNF R 1 associated death domain protein ( TRADD ) intracellularly , although it can be detected at low levels at the plasma membrane , indicating that most of LMP 1 ' s signaling complex resides in intracellular compartments . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Tumor necrosis factor receptor 1 ( TNFR 1 ) associated death domain protein ( TRADD ) is essential in recruiting signaling molecules to the TNFR 1 receptor complex . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| In order to determine whether osteosarcomas display an increased frequency of genetic alterations that affect apoptosis signaling , we analyzed the death domains of the death receptor genes CD95 / Fas / Apo1 , TNFR 1 , DR3 / Apo3 / WSL 1 / LARD / TRAMP , DR5 / TRAIL R2 / TRICK2 / KILLER , DR 6 and the complete coding sequences of the death receptor gene DR4 / TRAIL R 1 and the genes of the adaptors TRADD and FADD / MORT 1 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| We examined expression and interactions of the TNFR 1 binding proteins , DENN / MADD , and TNFR associated death domain ( TRADD ) protein in AD affected tissues and cell cultures . ^^^ Conversely , TRADD , TNFR 1 , and activated JNK were increased . ^^^ DENN / MADD and TRADD competitively bound to TNFR 1 when overexpressed in N ( 2 ) A cells , with DENN / MADD abrogating TNFR 1 binding to TRADD . ^^^ Reduction of DENN / MADD may affect long term neuronal viability in AD by allowing TRADD mediation of TNFR 1 signaling in response to oxidative or cytokine promoted stresses . . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ A proline rich region ( amino acids 796 807 ) is critical for maintaining AIP 1 in a closed form , which associates with a region of TNFR 1 distinct from the death domain , the site of TNFR 1 association with TRADD . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| Consistent with this , WT and mutant full length TNFRSF1A formed cytoplasmic aggregates that co localized with ubiquitin and chaperones , and with the signal transducer TRADD , but not with the inhibitor , silencer of death domain ( SODD ) . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| We demonstrate here that within minutes internalized TNF R 1 ( TNF receptosomes ) recruits TRADD , FADD , and caspase 8 to establish the `` death inducing signaling complex ' ' ( DISC ) . ^^^ In contrast , aggregation of TRADD , FADD , and caspase 8 to establish the TNF R 1 associated DISC is critically dependent on receptor endocytosis . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| These cytokines induce cell death through sequential recruitment by the death receptors TNFR 1 associated death domain protein ( TRADD ) , Fas associated death domain protein ( FADD ) , FADD like interleukin 1beta converting enzyme ( FLICE ) , and downstream caspases . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| This was established by showing that CIN 85 was co precipitated with TNFR 1 , TRADD , cIAP 1 and TARF1 / 2 , but not with FADD , RIP , caspase 8 or TRAF 6 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| CRT on RK ( 13 ) cell surface ( srCRT ) forms complex ( es ) with tumor necrosis factor receptor 1 ( TNFR 1 ) and TNFR associated death domain ( TRADD ) protein of the cell membrane . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 . ^^^ |
|
| Interacting proteins: Q15628 and P19438 |
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 P19438 |
Pubmed |
SVM Score :0.0 |
| The TNFR associated death domain ( TRADD ) protein has been suggested to be a crucial signal adaptor that mediates all intracellular responses from TNFR 1 . ^^^ We found that TRADD is required for TNFR 1 to induce NF kappaB activation and caspase 8 dependent apoptosis but is dispensable for TNFR 1 initiated , RIP 1 dependent necrosis . ^^^ Our data also show that TRADD and RIP 1 compete for recruitment to the TNFR 1 signaling complex and the distinct programs of cell death . ^^^ Thus , TNFR 1 initiated intracellular signals diverge at a very proximal level by the independent association of two death domain containing proteins , RIP 1 and TRADD . ^^^ |
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| Interacting proteins: Q15628 and P19438 |
Pubmed |
SVM Score :0.0 |
| K 17 interacts with TNF receptor 1 ( TNFR 1 ) associated death domain protein ( TRADD ) , a death adaptor essential for TNFR 1 dependent signal relay , suggesting a functional link between this keratin and TNFalpha signaling . ^^^ |
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| Interacting proteins: Q15628 and P19438 |
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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