| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2047951 | FEBS Letters | 2011 | 5 Pages |
Proteins of the Bcl-2 family regulate programmed cell death in mammals by promoting the release of cytochrome c from mitochondria in response to various proapoptotic stimuli. The mechanism by which BH3-only members of the family activate multidomain proapoptotic proteins Bax and Bak to form a pore in mitochondrial membranes remains under dispute. We report that cell death promoting activity of BH3-only protein Bim can be reconstituted in yeast when both Bax and antiapoptotic protein Bcl-XL are present, suggesting that Bim likely activates Bax indirectly by inhibiting antiapoptotic proteins.
► BH3-only protein Bim was studied by coexpression with other Bcl-2 proteins in yeast. ► In this model, Bim activates Bax/Bak indirectly by inhibition of Bcl-XL/Bcl-2. ► Activity of Bim is not dependent on the presence of VDAC in the outer mitochondrial membrane.
