A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions. |
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| Authors: | T Chittenden C Flemington A B Houghton R G Ebb G J Gallo B Elangovan G Chinnadurai and R J Lutz |
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| Affiliation: | Apoptosis Technology, Inc., Cambridge, MA 02139, USA. |
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| Abstract: | 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. |
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