Members in the BCL-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. BCL-2 homology 3 (BH3) domain is a potent death domain. BH3 domain containing pro-apoptotic proteins, including BAD, BAX, BID, BIK, HRK, NIP3, and BIM, form a growing subclass of the BCL-2 family. A novel BH3 domain containing protein was recently identified and designated Bnip3L, Bnip3, and NIX (for NIP3-like protein X). Bnip3L/Bnip3/Nix is a homolog of the E1B 19K/BCL-2 binding and pro-apoptotic protein Bnip3. Overexpression of Bnip3L induces apoptosis. Bnip3L interacts with and overcomes suppression by BCL-2 and BCL-XL. Bnip3L is localized in mitochondria. The messenger RNA of Bnip3L is ubiquitously expressed in human tissues. Bnip3L and Bnip3 form a new subfamily of the pro-apoptotic mitochondrial proteins.
BNIP3L; BCL2/adenovirus E1B 19kDa interacting protein 3-like; BCL2/adenovirus E1B 19kD interacting protein 3 like; BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like; BNIP3a; Nix; NIP3L; NIP3-like protein X; adenovirus E1B19k-binding protein B5; BCL2/adenovirus E1B 19-kd protein-interacting protein 3a; BCL2/adenovirus E1B 19 kDa protein-interacting protein 3A