Tumor necrosis factor (TNF) activates TNF receptor-1 (TNFR1), leading to diverse biological activities in many cell types. TNFR1 contains an intracellular death domain that is required for signaling related to antiviral activity, programmed cell death, and NF-κB activation. TNFR1-associated death domain protein (TRADD) was isolated in a screen to identify proteins that interact with the death domain of TNFR1. TRADD is a 34-kDa protein that contains a 111-amino acid death domain with sequence similarity to TNFR1. This domain mediates oligomerization of TRADD and interaction with TNFR1. TRADD mRNA is expressed ubiquitously, and overexpression of TRADD causes TNF-induced apoptosis and activation of NF-κB. These responses require the TRADD death domain. In addition to TNF signaling, TRADD N-terminus can interact with Stat1 in response to IFNγ, and this interaction can negatively regulate Stat activity.
Wesemann, D.R. et al. (2004) Nat. Immun. 5:199.
Hsu, H. et al. (1995) Cell 81:495.
*For more information, see UniProt Accession Q15628
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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