| First Author | Chittenden T | Year | 1995 |
| Journal | EMBO J | Volume | 14 |
| Issue | 22 | Pages | 5589-96 |
| PubMed ID | 8521816 | Mgi Jnum | J:43660 |
| Mgi Id | MGI:1098203 | Doi | 10.1002/j.1460-2075.1995.tb00246.x |
| Citation | Chittenden T, et al. (1995) A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions. EMBO J 14(22):5589-96 |
| abstractText | Regulation of the cell death program involves physical interactions between different members of the Bcl-2 family that either promote or suppress apoptosis. The Bcl-2 homolog, Bak, promotes apoptosis and binds anti-apoptotic family members including Bcl-2 and Bcl-xL. We have identified a domain in Bak that is both necessary and sufficient for cytotoxic activity and binding to Bcl-xL. Sequences similar to this domain were identified in Bax and Bip1, two other proteins that promote apoptosis and interact with Bcl-xL, and were likewise critical for their capacity to kill cells and bind Bcl-xL. Thus, the domain is of central importance in mediating the function of multiple cell death-regulatory proteins that interact with Bcl-2 family members. |
