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.
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]