Abstract
FADD/MORT1 is a death domain (DD)-containing adaptor/signaling molecule that interacts with the intracellular DD of FAS/APO-I (CD95) and tumor necrosis factor receptor 1 and the prodomain of caspase-8 (Mch5/MACH/FLICE). FADD engagement of caspase-8 presumably activates this caspase and leads to apoptosis. Another DD-containing adaptor/signaling molecule, CRADD, was identified and was shown to induce apoptosis. CRADD has a dual-domain structure similar to that of FADD. It has an NH2-terminal caspase homology domain that interacts with caspase-2 and a COOH-terminal DD that interacts with RIP. CRADD is constitutively expressed in many tissues and thus could play a role in regulating apoptosis in mammalian cells.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adaptor Proteins, Signal Transducing*
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Adult
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Amino Acid Sequence
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Apoptosis / physiology*
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Base Sequence
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CRADD Signaling Adaptor Protein
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Carrier Proteins / genetics*
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Carrier Proteins / isolation & purification
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Carrier Proteins / metabolism
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Cysteine Endopeptidases / genetics
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Cysteine Endopeptidases / metabolism
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Fas Ligand Protein
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Fas-Associated Death Domain Protein
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Fetus
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Humans
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / metabolism
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Molecular Sequence Data
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Proteins / genetics*
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Proteins / isolation & purification
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Proteins / metabolism
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Receptor-Interacting Protein Serine-Threonine Kinases
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Receptors, Tumor Necrosis Factor / genetics
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Receptors, Tumor Necrosis Factor / metabolism
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Sequence Homology, Amino Acid
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fas Receptor / genetics
Substances
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Adaptor Proteins, Signal Transducing
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CRADD Signaling Adaptor Protein
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CRADD protein, human
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Carrier Proteins
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FADD protein, human
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FASLG protein, human
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Fas Ligand Protein
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Fas-Associated Death Domain Protein
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Membrane Glycoproteins
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Proteins
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Receptors, Tumor Necrosis Factor
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fas Receptor
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RIPK1 protein, human
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Receptor-Interacting Protein Serine-Threonine Kinases
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Cysteine Endopeptidases