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PMID:8358790
| Citation |
Oltvai, ZN, Milliman, CL and Korsmeyer, SJ (1993) Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74:609-19 |
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| Abstract |
Bcl-2 protein is able to repress a number of apoptotic death programs. To investigate the mechanism of Bcl-2's effect, we examined whether Bcl-2 interacted with other proteins. We identified an associated 21 kd protein partner, Bax, that has extensive amino acid homology with Bcl-2, focused within highly conserved domains I and II. Bax is encoded by six exons and demonstrates a complex pattern of alternative RNA splicing that predicts a 21 kd membrane (alpha) and two forms of cytosolic protein (beta and gamma). Bax homodimerizes and forms heterodimers with Bcl-2 in vivo. Overexpressed Bax accelerates apoptotic death induced by cytokine deprivation in an IL-3-dependent cell line. Overexpressed Bax also counters the death repressor activity of Bcl-2. These data suggest a model in which the ratio of Bcl-2 to Bax determines survival or death following an apoptotic stimulus. |
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| Keywords |
Amino Acid Sequence; Animals; Apoptosis; Base Sequence; Blotting, Western; Cell Line; Cloning, Molecular; Conserved Sequence; Humans; Macromolecular Substances; Mice; Molecular Sequence Data; Polymerase Chain Reaction/methods; Proto-Oncogene Proteins/genetics; Proto-Oncogene Proteins/isolation & purification; Proto-Oncogene Proteins/metabolism; Proto-Oncogene Proteins c-bcl-2; Restriction Mapping; Sequence Homology, Amino Acid; bcl-2-Associated X Protein |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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See also
References
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