Is MAC the knife that cuts cytochrome c from mitochondria during apoptosis?

L. M. Dejean, S. Martinez-Caballero, K. W. Kinnally

Research output: Contribution to journalReview articlepeer-review


Apoptosis is a phenomenon fundamental to higher eukaryotes and essential to mechanisms controlling tissue homeostasis. Bcl-2 family proteins tightly control this cell death program by regulating the permeabilization of the mitochondrial outer membrane and, hence, the release of cytochrome c and other proapoptotic factors. Mitochondrial apoptosis-induced channel (MAC) is the mitochondrial apoptosis-induced channel and is responsible for cytochrome c release early in apoptosis. MAC activity is detected by patch clamping mitochondria at the time of cytochrome c release. The Bcl-2 family proteins regulate apoptosis by controlling the formation of MAC. Depending on cell type and apoptotic inducer, Bax and/or Bak are structural component(s) of MAC. Overexpression of the antiapoptotic protein Bcl-2 eliminates MAC activity. The focus of this review is a biophysical characterization of MAC activity and its regulation by Bcl-2 family proteins, and ends with some discussion of therapeutic targets.

Original languageEnglish (US)
Pages (from-to)1387-1395
Number of pages9
JournalCell Death and Differentiation
Issue number8
StatePublished - Aug 2006


  • Apoptosis
  • Bax
  • Bcl-2
  • Cytochrome c
  • MAC
  • Mitochondrial apoptosis-induced channel
  • Patch-clamp
  • t-Bid

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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