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Uncovering the connection between DED and apoptosis: why is it key to cell signaling?
Death effector domain (DED) is a unique protein interaction domain that only exists in eukaryotes and can regulate a variety of cell signaling pathways. This domain is found in inactive procaspases and in proteins involved in regulating the apoptotic cascade, such as proteins with FAS-binding death domains (FADD). Current research shows that DED's critical role in cell life and death decisions is not limited to apoptosis.
The structure of DED reveals its importance in apoptosis and other cellular processes.
Structure
DED is a subfamily of the death domain superfamily. Its structure consists of six α-helices, which makes it similar to other structures, such as the caspase recruitment domain (CARD) and the pyridine domain (PYD). and Death Domain (DD). Although these subfamilies differ in side features, their basic α-helical structures are similar.
Function
Extrinsic apoptosis
Apoptosis is a controlled and programmed cell death process that has significant advantages over the life cycle of an organism. The extrinsic apoptotic pathway is directed by a family of proteases that become activated in response to death stimuli. It is crucial to understand the role of DED in this process, particularly in the formation of the death signaling complex (DISC).
FADD's DED forms a stable structure through self-aggregation, which promotes the transmission of lethal signals.
During the formation of DISC, the interaction between pro-caspase-8 (pro-caspase-8) and FADD is critical for the initiation of apoptosis. This interaction leads to the dimerization of pro-caspase, leading to its activation and ultimately execution of cell death.
Necroptosis
Notably, المقدار pro-caspase-8 can also heterodimerize with another protein with DED, FLIPL. FLIPL's British caspase is not sufficient to initiate the typical apoptotic process, but it can guide necroptosis. This phenomenon highlights the complexity and bidirectional nature of DED's role in cellular life and death.
The DED protein family includes caspase-8, caspase-10, FLICE-like inhibitory protein, etc. These proteins play a pivotal role in apoptosis and other cellular processes.
DED protein family
The most famous protein families included in DED are caspase-8 and caspase-10. These enzymes not only perform structural decomposition of cells during apoptosis, but also participate in the regulation of cell life and death. Similarly, FLICE-like inhibitory protein (c-FLIP) can prevent the signaling of death receptors, thereby preventing the occurrence of apoptosis.
Clinical Application
Understanding how DED and its complexes act in cellular processes of life and death could help treat a variety of diseases, including cancer. When the process of apoptosis is abnormal, it may lead to various pathological conditions such as cancer, inflammation, and neurodegenerative diseases. Future therapeutic strategies may target DED-related pathways to promote damaged cell death and restoration of physiological balance.
Scientists committed to exploring DED are working hard to reveal its potential role in different diseases. So, what new treatment possibilities will DED reveal in future medical research?
