The Bcl-2 family proteins plays a central role in apoptosis. The pro- or anti-apoptotic activities of Bcl-2 family are dependent on the Bcl-2 homology (BH) regions. Bcl-rambo, a new pro-apoptotic member, is unusual in that its pro-apoptotic activity is independent of its BH domains. However, the mechanism underlying Bcl-rambo-induced apoptosis is largely unknown. Mitochondrial localization is indispensable for the pro-apoptotic function of Bcl-rambo. Bcl-rambo interacts physically with the adenine nucleotide translocator (ANT), suppresses the ADT/ATP-dependent translocation activity of ANT. Collectively, our data indicate Bcl-rambo is a pro-apoptotic member of the Bcl-2 family, induces the permeability transition via interaction with ANT. Structured summary of protein interactions:: Bcl-Rambo and HSP60 colocalize by fluorescence microscopy (View interaction) Bcl-rambo binds to ANT1 by pull down (View interaction). © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Kim, J. Y., So, K. J., Lee, S., & Park, J. H. (2012). Bcl-rambo induces apoptosis via interaction with the adenine nucleotide translocator. FEBS Letters, 586(19), 3142–3149. https://doi.org/10.1016/j.febslet.2012.08.015