The BH3-only proteins, which include Blk, Bad, Bik, Hrk, BID, Bim, NOXA, PUMA and Bmf, are proapoptotic members of the Bcl-2 family. Bcl-2 modifying factor (Bmf) is a BH3-only protein that binds prosurvival Bcl-2 family members to initiate apoptosis. Bmf is sequestered to Myosin V motors on Actin in the cytoskeleton by associating with Dynein light chain 2 (DLC2) homodimers. If the cell undergoes loss of attachment (anoikis), the cytoskeleton is disrupted and Bmf is released from DLC2. Bmf then translocates to the mitochondria, where Bcl-2 (an anti-apoptotic family member) is sequestered. The BH3 domain of Bmf facilitates binding to a hydrophobic groove on the surface of Bcl-2. Binding results in a caspase cascade leading to apoptosis. Bmf is widely expressed in tissues such as pancreas, liver and kidney, and in hematopoietic tissues. The gene encoding Bmf maps to chromosome 15q14.