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• W2022247016 endingPage "13978" @default.
• W2022247016 startingPage "13973" @default.
• W2022247016 abstract "The two cell surface receptors for tumor necrosis factor (TNF) interact with a number of intracellular signal transducing proteins. The association of TRADD, a 34-kDa cytoplasmic protein containing a C-terminal death domain, with aggregated TNF receptor 1 (TNF-R1) through their respective death domains leads to NF-kappa B activation and programmed cell death. In contrast, TNF receptor 2 (TNF-R2) interacts with the TNF receptor associated factors 2/1 (TRAF2/TRAF1) heterocomplex, which mediates the recruitment of two cellular inhibitor of apoptosis proteins (c-IAP1 and c-IAP2) to TNF-R2. Here we show that the TNF-R2 signal transducers TRAF2 and c-IAP1 are a part of the TNF-R1 signaling complex. The recruitment of TRAF2 and c-IAP1 to TNF-R1 is TNF-dependent, is mediated by TRADD, and is independent of TNF-R2. These data establish the physiological involvement of TRAF2 and c-IAP1 in TNF-R1 signaling and help provide a molecular explanation for both the overlapping and distinct signals generated by the two TNF receptors." @default.
• W2022247016 created "2016-06-24" @default.
• W2022247016 creator A5052763825 @default.
• W2022247016 creator A5076136934 @default.
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• W2022247016 date "1996-11-26" @default.
• W2022247016 modified "2023-10-10" @default.
• W2022247016 title "The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex" @default.
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• W2022247016 doi "https://doi.org/10.1073/pnas.93.24.13973" @default.
• W2022247016 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/19479" @default.
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