FADD or Fas-Associated protein with Death Domain is an adaptor molecule that mediates death signaling by the Fas-receptor, tumor necrosis factor receptor and TRAIL-receptor. FADD binds to these receptors via the C-terminus Death Domain which then unmasks the N-terminal effector domain of FADD thereby allowing it to recruit caspase-8 and activate the cysteine protease cascade leading to apoptosis. Cells lacking FADD are defective in intracellular double-stranded RNA (dsRNA)-activated gene expression, including production of type I (alpha/beta) interferons and are thus very susceptible to viral infection.
Vertebrate innate immunity provides a first line of defence against pathogens such as viruses and bacteria. Viral infection activates a potent innate immune response, which can be triggered by double-stranded (ds)RNA produced during viral replication. Here, we report that mammalian
Fas-associated death domain protein (FADD) is an adaptor molecule that bridges the interactions between membrane death receptors and initiator caspases. Thus, the site of its action has always been expected to be the cytoplasmic death-inducing signaling complex (DISC). Recent evidence
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