Activation of cell death by Bad.
In the latest issue of Molecular Cell, the Andrews lab provide the first evidence that the complexes of Bcl-2 family proteins, which regulate mitochondrial outer membrane permeabilization and thereby cell death, are not necessarily dimeric. Instead Bad binds a pre-existing membrane bound hetero-trimer consisting of a dimer of Bcl-XL and one tBid, promoting an allosteric change in the complex that lifts tBid away from the membrane enabling the bound tBid to activate Bax to kill the cell.
