Description
Product Characteristics:
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.
Subcellular location: Cytoplasm, Cell membrane
Synonyms: Bcl 2 modying factor, Bcl-2-modying factor, Bcl2 modying factor, Bmf, BMF_HUMAN, FLJ00065.
Target Information: The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein contains a single BCL2 homology domain 3 (BH3), and has been shown to bind BCL2 proteins and function as an apoptotic activator. This protein is found to be sequestered to myosin V motors by its association with dynein light chain 2, which may be important for sensing intracellular damage and triggering apoptosis. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]