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Apoptotic cell death occurs through activation of procaspases, the precursors of a group of aspartate-specific cysteine proteases known as caspases. Procaspase activation is mediated by death adapter proteins such as the mammalian proteins FADD and Apaf-1 and theCaenorhabditis elegans protein CED-4. These adapters bind to procaspases and facilitate oligomerization and subsequent auto-proteolytic processing of the zymogens. Here we report cloning and characterization of dFADD, a FADD homologue inDrosophila. dFADD contains a death domain that is highly homologous to the FADD death domain, and it also shares a novel domain with a Drosophila caspase DREDD, which we call death-inducing domain. dFADD binds to DREDD through the death-inducing domain and enhances the cell death activity and proteolytic processing of DREDD. dFADD and DREDD are stabilized by their interaction. The …