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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.

Pubmed ID: 9267021


  • Zou H
  • Henzel WJ
  • Liu X
  • Lutschg A
  • Wang X



Publication Data

August 8, 1997

Associated Grants


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