NMR structure and mutagenesis of the FADD (Mort1) death-effector domain

Article Abstract:

Neither wild-type death-effector domain (DED) of the adaptor protein FADD, nor full-length FADD can be obtained in a suitable form for study by nuclear magnetic resonance. Several site-directed mutants have been prepared and screened, for ability to be expressed as a soluble protein, bind to caspase (FLICE) and induce apoptosis. Phe25-Tyr (F25Y) was the mutant protein chosen for structure determination. Mutations inhibiting protein-protein interactions involving the Fas death domain had no effect on introduction into the FADD death-effector domain.

Usage, Magnetic resonance imaging, Mutagenesis

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Cell-autonomous Fas (CD95)/Fas-ligand interaction mediates activation-induced apoptosis in T-cell hybridomas

Article Abstract:

Examination of apoptosis by various murine T-cell hybridomas indicates that activation of T-cell hybridomas induces rapid expression of Fas/CD95 receptor, which on ligation transduce a potent apoptotic signal. Activation-induced apoptosis is inhibited by modulating the Fas/Fas-ligand interaction. Stimulation of apoptosis in a single T hybridoma cell by T-cell receptor ligation reveals that cell death can be stimulated by the Fas/Fas-ligand interaction in a cell-autonomous manner.

Genetic aspects

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Induction of apoptosis in mature T cells by tumour necrosis factor

Article Abstract:

The death of mature T cells can occur due to two different molecular mechanisms, tumor necrosis factor (TNF) and the Fas Ligand. TNF acts as an intermediary in T-cell death that occurs by T-cell receptor induction, and blockage of TNF and the Fas ligand are necessary to stop T-cell death. Immune responses are modulated by T cell receptor-induced apoptosis and can occur due to interactions between Fas and the Fas ligand.

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