Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer (reviewed in 1). The Bcl-2 family of proteins is comprised of critical regulators of apoptosis that can be divided into two classes: those that inhibit apoptosis and those that promote cell death (reviewed in 2 and 3). Bid, a pro-apoptotic Bcl-2 family member, is cleaved by caspase-8 in response to apoptotic signals (4,5), exposing the Bcl-2 homology 3 (BH3) domain which is normally buried in the full-length protein (6). The cleaved complex is myristoylated and translocated to the mitochondrial membrane where it may induce mitochondrial Bax and Bak to oligomerize (7,8).