The Death Effector Domain (DED) is a protein interaction domain found in various proteins involved in apoptosis, a form of programmed cell death. The DED domain is crucial for the formation of death-inducing signaling complexes (DISCs) that initiate the apoptotic cascade. This article delves into the background of DED-containing proteins, particularly focusing on human recombinant versions.
DEDs are typically found in proteins such as Fas-associated death domain protein (FADD), caspase-8, and caspase-10. These domains facilitate protein-protein interactions necessary for the apoptotic signaling pathways. The DED domain is characterized by a conserved sequence that allows it to bind to other DED-containing proteins, forming complexes that activate downstream apoptotic signals .
The primary function of DED-containing proteins is to mediate the formation of DISCs. Upon activation by death receptors such as Fas, FADD is recruited to the receptor complex. FADD then binds to procaspase-8 and procaspase-10 through its DED, facilitating their activation. Once activated, these caspases cleave various substrates, leading to the execution phase of apoptosis .
The dysregulation of DED-containing proteins has been implicated in various diseases, including cancer. For instance, overexpression of FADD has been associated with increased cancer cell proliferation and resistance to apoptosis. Understanding the role of DED-containing proteins in apoptosis can provide insights into potential therapeutic targets for cancer treatment .