| First Author | Lindenboim L | Year | 2005 |
| Journal | Cell Death Differ | Volume | 12 |
| Issue | 7 | Pages | 713-23 |
| PubMed ID | 15861188 | Mgi Jnum | J:111864 |
| Mgi Id | MGI:3654979 | Doi | 10.1038/sj.cdd.4401638 |
| Citation | Lindenboim L, et al. (2005) Bak but not Bax is essential for Bcl-xS-induced apoptosis. Cell Death Differ 12(7):713-23 |
| abstractText | Bcl-x(S), a proapoptotic member of the Bcl-2 protein family, is localized in the mitochondria and induces apoptosis in a caspase- and BH3-dependent manner by a mechanism involving cytochrome c release. The way in which Bcl-x(S) induces caspase activation and cytochrome c release, as well as the relationship between Bcl-x(S) and other proapoptotic members of the Bcl-2 family, is not known. Here we used embryonic fibroblasts derived from mice deficient in the multidomain proapoptotic members of the Bcl-2 family (Bax and Bak) and the apoptotic components of the apoptosome (Apaf-1 and caspase-9) to unravel the cascade of events by which Bcl-x(S) promotes apoptosis. Our results show that Bak but not Bax is essential for Bcl-x(S)-induced apoptosis. Bcl-x(S) induced activation of Bak, which in turn promoted apoptosis by apoptosome-dependent and -independent pathways. These findings provide the first evidence that a proapoptotic Bcl-2 family protein induces apoptosis exclusively via Bak. |
