BCL-2 alpha encodes a novel small molecular weight GTP binding protein.
Despite little sequence homology other than the GDP/GTP binding region, bcl-2 and ras proteins behave in similar fashion in many physiological and biochemical aspects. Both of them are toxin insensitive, small Mr G-proteins attached to the inner surface of the cell membrane with autophosphorylation activity and can cooperate with c-myc in cell transformation. In the case of bcl-2, however, the mechanism of activation is still unclear. One possibility is that, following antigen or mitogen stimulation, the bcl-2 protein is activated by nucleotide exchange; then the activated bcl-2 protein may interact with some other protein in the signal transduction pathway leading to cell proliferation. Dissection of the role of bcl-2 in the regulation of B-cell proliferation will be an important step in understanding its role in the pathogenesis of B-cell neoplasia.
Haldar
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Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA 19140.
Beatty
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Croce
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D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000235:genetics* / Q000378:metabolism; D011905:Genes, ras; D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012689:Sequence Homology, Nucleic Acid; D015398:Signal Transduction
D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins