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  • Title: BH3 domain of BAD is required for heterodimerization with BCL-XL and pro-apoptotic activity.
    Author: Zha J, Harada H, Osipov K, Jockel J, Waksman G, Korsmeyer SJ.
    Journal: J Biol Chem; 1997 Sep 26; 272(39):24101-4. PubMed ID: 9305851.
    Abstract:
    BAD interacts with anti-apoptotic molecules BCL-2 and BCL-XL and promotes apoptosis. BAD is phosphorylated on serine residues in response to a survival factor, interleukin-3. Phosphorylated BAD cannot bind to BCL-XL or BCL-2 at membrane sites and is found in the cytosol bound to 14-3-3. We report here that deletion mapping and site-directed mutagenesis identified a BH3 domain within BAD that proved necessary for both its heterodimerization with BCL-XL and its death agonist activity. Substitution of the conserved Leu151 with Ala in the BH3 amphipathic alpha-helix abrogated both functions. The BAD Leu151 mutant was predominantly in the cytosol bound to 14-3-3. The BH3 domain of BCL-2 also proved important for BCL-2/BAD interaction. These results establish a critical role for a BH3 domain within BAD and provide evidence that BAD may function as a death ligand whose pro-apoptotic activity requires heterodimerization with BCL-XL.
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