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      Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death.

      1 , ,
      Cell
      Elsevier BV

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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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          Author and article information

          Journal
          Cell
          Cell
          Elsevier BV
          0092-8674
          0092-8674
          Aug 27 1993
          : 74
          : 4
          Affiliations
          [1 ] Howard Hughes Medical Institute Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
          Article
          0092-8674(93)90509-O
          10.1016/0092-8674(93)90509-o
          8358790
          0949b6e1-a9bf-42f5-abb9-1d80ce7d08e4
          History

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