Apoptotic signals are often triggered by cell surface death receptors through protein-protein interactions mediated by conserved domains such as the death effector domain (1). A novel death effector domain (DED)-containing protein, DEDD2, has been recently identified and its over-expression in transfected cells induces moderate apoptosis and results in substantial sensitization to apoptosis induced by Fas, TRAIL, and FADD (2). More recently, work has shown that DEDD2 can bind caspase-8 and -10 in addition to FLIP but not FADD (2,3). Like the related protein DEDD, DEDD2 translocates from the cytosol to the nucleus upon induction of apoptosis, and it has been suggested that DEDD2 may target caspase-8 to the nucleus and that DEDD2 thus plays a critical role in death receptor-induced apoptosis (3). At least two alternatively spliced transcript variants encoding distinct isoforms have been found for DEDD2.
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