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J Biol Chem, Vol. 274, Issue 1, 7-10, January 1, 1999
From the Manitoba Institute of Cell Biology, University of
Manitoba, Winnipeg, Manitoba R3E 0V9, Canada
We have identified Nix, a homolog of the E1B
19K/Bcl-2 binding and pro-apoptotic protein Nip3. Human and murine Nix
have a 56 and 53% amino acid identity to human and murine Nip3,
respectively. The carboxyl terminus of Nix, including a transmembrane
domain, is highly homologous to Nip3 but it bears a longer and distinct asparagine/proline-rich N terminus. Human Nip3 maps to chromosome 14q11.2-q12, whereas Nix/BNip3L was found on 8q21. Nix encodes a
23.8-kDa protein but it is expressed as a 48-kDa protein, suggesting that it homodimerizes similarly to Nip3. Following transfection, Nix
protein undergoes progressive proteolysis to an 11-kDa C-terminal fragment, which is blocked by the proteasome inhibitor lactacystin. Nix
colocalizes with the mitochondrial matrix protein HSP60, and removal of
the putative transmembrane domain (TM) results in general cytoplasmic
and nuclear expression. When transiently expressed, Nix and Nip3 but
not TM deletion mutants rapidly activate apoptosis. Nix can overcome
the suppressers Bcl-2 and Bcl-XL, although high levels of Bcl-XL expression will inhibit apoptosis. We
propose that Nix and Nip3 form a new subfamily of pro-apoptotic
mitochondrial proteins.
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Z. Chen, K. Guo, S. Y. Toh, Z. Zhou, and P. Li Mitochondria Localization and Dimerization Are Required for CIDE-B to Induce Apoptosis J. Biol. Chem., July 21, 2000; 275(30): 22619 - 22622. [Abstract] [Full Text] [PDF]
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J. Bae, C. P. Leo, S. Y. Hsu, and A. J. W. Hsueh MCL-1S, a Splicing Variant of the Antiapoptotic BCL-2 Family Member MCL-1, Encodes a Proapoptotic Protein Possessing Only the BH3 Domain J. Biol. Chem., August 11, 2000; 275(33): 25255 - 25261. [Abstract] [Full Text] [PDF]
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