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Bad, a heterodimeric partner for Bcl-xL and Bcl-2, displaces bax and promotes cell death
Open accessAbstract
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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Metadata
- Authors
- Yang, E., Zha, J., Jockel, J., Boise, L. H., Thompson, C. B., & Korsmeyer, S. J.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1995-01
- Volume
- 80
- Issue
- 2
- Pages
- 285-291
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2057713336
- Cited by
- 2,100
- References
- 1
- FWCI
- 46.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
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