Casper is a FADD- and caspase-related inducer of apoptosis.

Caspases are cysteine proteases that play a central role in apoptosis. Caspase-8 may be the first enzyme of the proteolytic cascade activated by the Fas ligand and tumor necrosis factor (TNF). Caspase-8 is recruited to Fas and TNF receptor-1 (TNF-R1) through interaction of its prodomain with the death effector domain ...
(DED) of the receptor-associating FADD. Here we describe a novel 55 kDa protein, Casper, that has sequence similarity to caspase-8 throughout its length. However, Casper is not a caspase since it lacks several conserved amino acids found in all caspases. Casper interacts with FADD, caspase-8, caspase-3, TRAF1, and TRAF2 through distinct domains. When overexpressed in mammalian cells, Casper potently induces apoptosis. A C-terminal deletion mutant of Casper inhibits TNF- and Fas-induced cell death, suggesting that Casper is involved in these apoptotic pathways.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Antigens, CD95, Apoptosis, CASP8 and FADD-Like Apoptosis Regulating Protein, Carrier Proteins, Caspase 3, Caspase 8, Caspase 9, Caspases, Cloning, Molecular, Cysteine Endopeptidases, Endopeptidases, Enzyme Induction, Fas-Associated Death Domain Protein, Hela Cells, Humans, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Protein Binding, Protein Processing, Post-Translational, Proteins, Recombinant Proteins, Sequence Alignment, Sequence Deletion, Sequence Homology, Amino Acid, Serpins, Signal Transduction, Structure-Activity Relationship, TNF Receptor-Associated Factor 1, TNF Receptor-Associated Factor 2, Tumor Necrosis Factor-alpha, Viral Proteins
Immunity
Date: Jun. 01, 1997
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