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Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death.

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.

Pubmed ID: 7834748

Authors

  • Yang E
  • Zha J
  • Jockel J
  • Boise LH
  • Thompson CB
  • Korsmeyer SJ

Journal

Cell

Publication Data

January 27, 1995

Associated Grants

  • Agency: NCI NIH HHS, Id: CA50239

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Antibodies
  • Apoptosis
  • Carrier Proteins
  • Cloning, Molecular
  • Humans
  • Macromolecular Substances
  • Mammals
  • Mice
  • Molecular Sequence Data
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Recombinant Proteins
  • Saccharomyces cerevisiae
  • Sequence Homology, Amino Acid
  • Transfection
  • bcl-Associated Death Protein
  • bcl-X Protein