death effector domain binding

Definition

Target type: molecularfunction

Binding to a DED domain (death effector domain) of a protein, a homotypic protein interaction module composed of a bundle of six alpha-helices that is related in structure to the death domain (DD). [GOC:ecd, InterPro:IPR001875]

Death effector domain (DED) binding is a crucial molecular interaction that plays a pivotal role in the regulation of apoptosis, a programmed cell death process essential for maintaining cellular homeostasis. DEDs are conserved protein-protein interaction domains found in a variety of proteins involved in apoptosis signaling pathways. These domains facilitate the assembly of protein complexes, which in turn orchestrate the execution of the apoptotic program. DED-containing proteins can interact with each other through their DEDs, forming homo- or hetero-dimers or even larger oligomers. This interaction is highly specific, ensuring that the correct proteins assemble into functional complexes. The formation of these complexes triggers a cascade of events, culminating in the activation of caspases, a family of cysteine proteases that execute the apoptotic program by cleaving specific cellular substrates. DED-mediated interactions are critical for the proper activation and regulation of caspases, ensuring that apoptosis is initiated only when necessary and proceeds in a controlled manner. Moreover, DED binding contributes to the precise localization of apoptotic signaling components within cells, enabling efficient and targeted execution of the apoptotic program. This intricate interplay of DED-mediated interactions underlines the critical role of DED binding in orchestrating the complex and tightly regulated process of apoptosis.'
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Proteins (2)

Compounds (16)