Regulation of the Apaf-1/caspase-9 apoptosome by caspase-3 and XIAP.

@article{Zou2003RegulationOT,
  title={Regulation of the Apaf-1/caspase-9 apoptosome by caspase-3 and XIAP.},
  author={Hua Zou and R Yang and Junshan Hao and Jean Wang and Chaohong C Sun and Stephen W. Fesik and Joe C. Wu and Kevin James Tomaselli and Robert C. Armstrong},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 10},
  pages={
          8091-8
        }
}
The apoptosome is a multiprotein complex comprising Apaf-1, cytochrome c, and caspase-9 that functions to activate caspase-3 downstream of mitochondria in response to apoptotic signals. Binding of cytochrome c and dATP to Apaf-1 in the cytosol leads to the assembly of a heptameric complex in which each Apaf-1 subunit is bound noncovalently to a procaspase-9 subunit via their respective CARD domains. Assembly of the apoptosome results in the proteolytic cleavage of procaspase-9 at the cleavage… CONTINUE READING

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