Journal article

Preservation of mitochondrial structure and function after Bid- or Bax-mediated cytochrome c release

O von Ahsen, C Renken, G Perkins, RM Kluck, E Bossy-Wetzel, DD Newmeyer

The Journal of Cell Biology | ROCKEFELLER UNIV PRESS | Published : 2000


Proapoptotic members of the Bcl-2 protein family, including Bid and Bax, can activate apoptosis by directly interacting with mitochondria to cause cytochrome c translocation from the intermembrane space into the cytoplasm, thereby triggering Apaf-1-mediated caspase activation. Under some circumstances, when caspase activation is blocked, cells can recover from cytochrome c translocation; this suggests that apoptotic mitochondria may not always suffer catastrophic damage arising from the process of cytochrome c release. We now show that recombinant Bid and Bax cause complete cytochrome c loss from isolated mitochondria in vitro, but preserve the ultrastructure and protein import function of m..

View full abstract

University of Melbourne Researchers