Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3.
We report here the purification and cDNA cloning of Apaf-1, a novel 130 kd protein from HeLa cell cytosol that participates in the cytochrome c-dependent activation of caspase-3. The NH2-terminal 85 amino acids of Apaf-1 show 21% identity and 53% similarity to the NH2-terminal prodomain of the Caenorhabditis elegans caspase, ... CED-3. This is followed by 320 amino acids that show 22% identity and 48% similarity to CED-4, a protein that is believed to initiate apoptosis in C. elegans. The COOH-terminal region of Apaf-1 comprises multiple WD repeats, which are proposed to mediate protein-protein interactions. Cytochrome c binds to Apaf-1, an event that may trigger the activation of caspase-3, leading to apoptosis.
Mesh Terms:
Amino Acid Sequence, Animals, Apoptotic Protease-Activating Factor 1, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Calcium-Binding Proteins, Caspase 3, Caspases, Cell Line, Cloning, Molecular, Cysteine Endopeptidases, Cytochrome c Group, Cytosol, DNA, Complementary, Enzyme Activation, Enzyme Precursors, Hela Cells, Helminth Proteins, Humans, Molecular Sequence Data, Proteins, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Transfection
Amino Acid Sequence, Animals, Apoptotic Protease-Activating Factor 1, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Calcium-Binding Proteins, Caspase 3, Caspases, Cell Line, Cloning, Molecular, Cysteine Endopeptidases, Cytochrome c Group, Cytosol, DNA, Complementary, Enzyme Activation, Enzyme Precursors, Hela Cells, Helminth Proteins, Humans, Molecular Sequence Data, Proteins, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Transfection
Cell
Date: Aug. 08, 1997
PubMed ID: 9267021
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