BNIP3L/Nix (D4R4B) Rabbit mAb

BCL2/Adenovirus E1B 19 kDa protein-interacting protein 3-like (BNIP3L) (1), also termed BNIP3α (2), B5 (3), and Nix (4), is a member of the Bcl-2 family of apoptotic regulators with highest homology to BNIP3. BNIP3L can bind BNIP3, Bcl-xL, and Bcl-2 (1-5). BNIP3L forms homodimers that withstand denaturing by SDS and reducing conditions (5). BNIP3L is a mitochondrial protein and knockout studies suggest that BNIP3L regulates autophagic clearance of damaged mitochondria during erythroid maturation via mitochondrial autophagy (6,7). It has been shown that the expression of BNIP3L is up-regulated during terminal erythroid differentiation (6-8), as well as in tumor cell lines during hypoxia (9-11). BNIP3L directly regulates the elimination of mitochondria through its ability to bind to and recruit important components of the autophagic machinery, including LC3/Atg8 and GABARAP proteins, via its amino-terminal LC3-interacting region (LIR) (12). BNIP3L may also indirectly activate phagophore formation either via the recruitment of autophagy proteins or by binding Bcl-xL, which in turn releases Beclin-1 (13). BNIP3L/Nix also plays a pivotal role in Parkin-mediated mitochondrial autophagy via its ability to mediate the mitochondrial translocation of Parkin (14). Activated BNIP3L can promote the opening of mitochondrial permeability transition pores resulting in mitochondrial depolarization, generation of reactive oxygen species, and induction of necrosis. Due to its involvement in cell death and autophagy, research scientists have implicated BNIP3L in heart disease and cancer (13). 1.Matsushima, M. et al. (1998) Genes Chromosomes Cancer 21, 230-5. 2.Yasuda, M. et al. (1999) Cancer Res 59, 533-7. 3.Ohi, N. et al. (1999) Cell Death Differ 6, 314-25. 4.Chen, G. et al. (1999) J Biol Chem 274, 7-10. 5.Imazu, T. et al. (1999) Oncogene 18, 4523-9. 6.Schweers, R.L. et al. (2007) Proc Natl Acad Sci USA 104, 19500-5. 7.Sandoval, H. et al. (2008) Nature 454, 232-5. 8.Aerbajinai, W. et al. (2003) Blood 102, 712-7. 9.Sowter, H.M. et al. (2001) Cancer Res 61, 6669-73. 10.Bruick, R.K. (2000) Proc Natl Acad Sci USA 97, 9082-7. 11.Fei, P. et al. (2004) Cancer Cell 6, 597-609. 12.Novak, I. et al. (2010) EMBO Rep 11, 45-51. 13.Zhang, J. and Ney, P.A. (2009) Cell Death Differ 16, 939-46. 14.Ding, W.X. et al. (2010) J Biol Chem 285, 27879-90.