Mitochondrial control of apoptosis: The role of cytochrome c

Jiyang Cai, Jie Yang, Dean P. Jones

Research output: Contribution to journalArticlepeer-review

675 Scopus citations


Mitochondrial cytochrome c (cyt c) has been found to have dual functions in controlling both cellular energetic metabolism and apoptosis. Through interaction with apoptotic protease activating factors (Apaf), cyt c can initiate the activation cascade of caspases once it is released into the cytosol. The loss of a component of the mitochondrial electron transport chain also triggers the generation of superoxide. Although cyt c can be released independent of the mitochondrial permeability transition (MPT), the accompanying cellular redox change can trigger the MPT. Since another apoptotic protease, AIF, is released by MPT, the two separate pathways provide redundancy that ensures effective execution of the cell death program. Anti-apoptotic Bcl-2 family proteins function as gatekeepers to prevent the release of both cyt c and AIF. In spite of their stabilization effect on the mitochondrial outer membrane, Bcl-2 proteins may also be involved in the direct binding of Apaf molecules as regulatory elements further downstream from the mitochondrial apoptotic signals. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)139-149
Number of pages11
JournalBiochimica et Biophysica Acta - Bioenergetics
Issue number1-2
StatePublished - Aug 10 1998
Externally publishedYes


  • Apaf
  • Apoptosis
  • Bcl-2
  • Caspase
  • Cytochrome c
  • Membrane potential
  • Mitochondrion
  • Oxidant-induced cell death
  • Permeability transition
  • Reactive oxygen species

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


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