[HTML][HTML] Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c–dependent activation of caspase-3
H Zou, WJ Henzel, X Liu, A Lutschg, X Wang - Cell, 1997 - cell.com
H Zou, WJ Henzel, X Liu, A Lutschg, X Wang
Cell, 1997•cell.comWe 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 NH 2-terminal 85 amino acids of Apaf-1 show 21% identity and 53% similarity to the NH
2-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 …
HeLa cell cytosol that participates in the cytochrome c–dependent activation of caspase-3.
The NH 2-terminal 85 amino acids of Apaf-1 show 21% identity and 53% similarity to the NH
2-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 …
Abstract
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.
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