Abstract
The death effector domain (DED) occurs in proteins that regulate programmed cell death. Both pro- and anti-apoptotic proteins containing DEDs have been identified. For Fas and possibly other death receptors, homotypic DED interactions connect the Fas-associated death domain (FADD) protein to caspase-8 and caspase-10 to mediate formation of the death-inducing signal complex. This complex can be inhibited by other DED-containing proteins. Accumulating evidence now suggests that DED-containing proteins have additional roles in controlling pathways of cellular activation and proliferation. Thus, the DED defines a family of proteins that may be pivotal to cellular homeostasis by establishing a 'cell renewal set point' that coregulates proliferation and apoptosis in parallel.
MeSH terms
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Adaptor Proteins, Signal Transducing*
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Amino Acid Sequence
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Animals
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Apoptosis / physiology*
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Carrier Proteins / metabolism
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Caspase 8
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Caspase 9
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Caspases / metabolism
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Cell Division / physiology
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DNA-Binding Proteins*
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Death Domain Receptor Signaling Adaptor Proteins
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Fas-Associated Death Domain Protein
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Homeostasis
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Humans
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Intracellular Signaling Peptides and Proteins
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Models, Biological
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Models, Molecular
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Molecular Sequence Data
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Protein Structure, Tertiary
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Proteins / chemistry*
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Proteins / genetics
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Proteins / physiology*
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Sequence Homology, Amino Acid
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Signal Transduction
Substances
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Adaptor Proteins, Signal Transducing
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Carrier Proteins
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DEDD protein, human
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DNA-Binding Proteins
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Death Domain Receptor Signaling Adaptor Proteins
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FADD protein, human
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Fas-Associated Death Domain Protein
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Intracellular Signaling Peptides and Proteins
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Proteins
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CASP8 protein, human
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CASP9 protein, human
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Caspase 8
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Caspase 9
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Caspases