Author: ["Alexei Degterev","Alexey Lugovskoy","Michael Cardone","Bradley Mulley","Gerhard Wagner","Timothy Mitchison","Junying Yuan"]
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Abstract
To study the role of the BH3 domain in mediating pro-apoptotic and anti-apoptotic activities of Bcl-2 family members, we identified a series of novel small molecules (BH3Is) that inhibit the binding of the Bak BH3 peptide to Bcl-xL. NMR analyses revealed that BH3Is target the BH3-binding pocket of Bcl-xL. Inhibitors specifically block the BH3-domain-mediated heterodimerization between Bcl-2 family members in vitro and in vivo and induce apoptosis. Our results indicate that BH3-dependent heterodimerization is the key function of anti-apoptotic Bcl-2 family members and is required for the maintenance of cellular homeostasis.Cite this article
Degterev, A., Lugovskoy, A., Cardone, M. et al. Identification of small-molecule inhibitors of interaction between the BH3 domain and Bcl-xL. Nat Cell Biol 3, 173–182 (2001). https://doi.org/10.1038/35055085 