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Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade.

We report here the purification of the third protein factor, Apaf-3, that participates in caspase-3 activation in vitro. Apaf-3 was identified as a member of the caspase family, caspase-9. Caspase-9 and Apaf-1 bind to each other via their respective NH2-terminal CED-3 homologous domains in the presence of cytochrome c and dATP, an event that leads to caspase-9 activation. Activated caspase-9 in turn cleaves and activates caspase-3. Depletion of caspase-9 from S-100 extracts diminished caspase-3 activation. Mutation of the active site of caspase-9 attenuated the activation of caspase-3 and cellular apoptotic response in vivo, indicating that caspase-9 is the most upstream member of the apoptotic protease cascade that is triggered by cytochrome c and dATP.

Pubmed ID: 9390557

Authors

  • Li P
  • Nijhawan D
  • Budihardjo I
  • Srinivasula SM
  • Ahmad M
  • Alnemri ES
  • Wang X

Journal

Cell

Publication Data

November 14, 1997

Associated Grants

  • Agency: NIA NIH HHS, Id: AG13487
  • Agency: NIGMS NIH HHS, Id: GM08014
  • Agency: NIGMS NIH HHS, Id: GMRO1-55942

Mesh Terms

  • Amino Acid Sequence
  • Apoptosis
  • Apoptotic Protease-Activating Factor 1
  • Binding Sites
  • Breast Neoplasms
  • Caspase 3
  • Caspase 9
  • Caspases
  • Cell Line
  • Cysteine Endopeptidases
  • Cytochrome c Group
  • Deoxyadenine Nucleotides
  • Enzyme Activation
  • Epithelial Cells
  • HeLa Cells
  • Humans
  • Kidney
  • Models, Chemical
  • Molecular Sequence Data
  • Multienzyme Complexes
  • Mutation
  • Protein Binding
  • Proteins
  • Tumor Cells, Cultured