Differential efflux of mitochondrial endonuclease G by hNoxa and tBid

Woo Seo Young, Sun Young Park, Cheol Won Yun, Tae Hyoung Kim

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


The Bcl-2 family of proteins regulates mitochondrial functions during cell death by modulating the efflux of death-promoting proteins such as cytochrome c and endonuclease G. Upon the binding of death ligands to their receptors, caspase-8 cleaves Bid, a BH3-only protein, into tBid that causes the mitochondrial damages resulting in the release of cytochrome c and endonuclease G. Also, another BH3-only protein, hNoxa, has been shown to induce the efflux of cytochrome c from the mitochondria. Whether the efflux proteins from the mitochondria in response to tBid or hNoxa are the same or different, however, has not been addressed. We have demonstrated that endonuclease G activities are not detectable among the proteins released from isolated mitochondria by hNoxa but are detectable in that by tBid. These results suggest that the efflux of proteins from the mitochondria are differentially modulated by tBid and hNoxa.

Original languageEnglish
Pages (from-to)556-559
Number of pages4
JournalJournal of Biochemistry and Molecular Biology
Issue number5
Publication statusPublished - 2006 Sept


  • Bid
  • Cytochrome c release
  • Endonuclease G
  • hNoxa

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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