alexa Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis.
Oncology

Oncology

Journal of Cancer Science & Therapy

Author(s): Li H, Zhu H, Xu CJ, Yuan J, Li H, Zhu H, Xu CJ, Yuan J

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Abstract We report here that BID, a BH3 domain-containing proapoptotic Bcl2 family member, is a specific proximal substrate of Casp8 in the Fas apoptotic signaling pathway. While full-length BID is localized in cytosol, truncated BID (tBID) translocates to mitochondria and thus transduces apoptotic signals from cytoplasmic membrane to mitochondria. tBID induces first the clustering of mitochondria around the nuclei and release of cytochrome c independent of caspase activity, and then the loss of mitochondrial membrane potential, cell shrinkage, and nuclear condensation in a caspase-dependent fashion. Coexpression of BclxL inhibits all the apoptotic changes induced by tBID. Our results indicate that BID is a mediator of mitochondrial damage induced by Casp8.
This article was published in Cell and referenced in Journal of Cancer Science & Therapy

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