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PMID:7834748
| Citation |
Yang, E, Zha, J, Jockel, J, Boise, LH, Thompson, CB and Korsmeyer, SJ (1995) Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell 80:285-91 |
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| Abstract |
To extend the mammalian cell death pathway, we screened for further Bcl-2 interacting proteins. Both yeast two-hybrid screening and lambda expression cloning identified a novel interacting protein, Bad, whose homology to Bcl-2 is limited to the BH1 and BH2 domains. Bad selectively dimerized with Bcl-xL as well as Bcl-2, but not with Bax, Bcl-xs, Mcl-1, A1, or itself. Bad binds more strongly to Bcl-xL than Bcl-2 in mammalian cells, and it reversed the death repressor activity of Bcl-xL, but not that of Bcl-2. When Bad dimerized with Bcl-xL, Bax was displaced and apoptosis was restored. When approximately half of Bax was heterodimerized, death was inhibited. The susceptibility of a cell to a death signal is determined by these competing dimerizations in which levels of Bad influence the effectiveness of Bcl-2 versus Bcl-xL in repressing death. |
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| Keywords |
Amino Acid Sequence; Animals; Antibodies; Apoptosis/physiology; Carrier Proteins/biosynthesis; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Cloning, Molecular; Humans; Macromolecular Substances; Mammals; Mice; Molecular Sequence Data; Proto-Oncogene Proteins/metabolism; Proto-Oncogene Proteins c-bcl-2; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Transfection; bcl-Associated Death Protein; bcl-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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