Direct Binding of Fas-associated Death Domain (FADD) to the Tumor Necrosis Factor-related Apoptosis-inducing Ligand Receptor DR5 Is Regulated by the Death Effector Domain of FADD
作者： Lance R. Thomas , Adrianna Henson , John C. Reed , Freddie R. Salsbury , Andrew Thorburn
关键词: Signal transducing adaptor protein 、 Cancer research 、 Fas ligand 、 Death effector domain 、 Death-inducing signaling complex 、 Signal transduction 、 Cell biology 、 Death domain 、 FADD 、 Chemistry 、 Fas receptor
摘要: Members of the tumor necrosis factor superfamily receptors induce apoptosis by recruiting adaptor molecules through death domain interactions. The central molecule for these is domain-containing protein Fas-associated (FADD). FADD binds a on receptor or additional and recruits caspases to activated receptor. Tumor factor-related apoptosis-inducing ligand (TRAIL) signals two receptors, DR4 DR5. Although there much interest in TRAIL, mechanism which recruited TRAIL not clear. Using reverse two-hybrid system we previously identified mutations effector that prevented binding Fas/CD95. Here show also prevent FADD-deficient Jurkat cells stably expressing did transduce Fas/CD95 signaling. Second site compensating restore signaling DR5 were domain. We conclude contrast current models where functions independently domain, comes into direct contact with both receptors.
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