Facilitation of mitochondrial outer and inner membrane permeabilization and cell death in oxidative stress by a novel Bcl-2 homology 3 domain protein.

@article{Szigeti2010FacilitationOM,
  title={Facilitation of mitochondrial outer and inner membrane permeabilization and cell death in oxidative stress by a novel Bcl-2 homology 3 domain protein.},
  author={Andr{\'a}s Szigeti and Eniko Hocs{\'a}k and Edit R{\'a}polti and B{\'o}gl{\'a}rka R{\'a}cz and Arp{\'a}d Boronkai and Eva Pozsgai and Balazs Debreceni and Zita Bognar and Szabolcs Bellyei and Bal{\'a}zs Sumegi and Ferenc Gallyas},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 3},
  pages={2140-51}
}
We identified a sequence homologous to the Bcl-2 homology 3 (BH3) domain of Bcl-2 proteins in SOUL. Tissues expressed the protein to different extents. It was predominantly located in the cytoplasm, although a fraction of SOUL was associated with the mitochondria that increased upon oxidative stress. Recombinant SOUL protein facilitated mitochondrial permeability transition and collapse of mitochondrial membrane potential (MMP) and facilitated the release of proapoptotic mitochondrial… CONTINUE READING