Bcl-rambo induces apoptosis via interaction with the adenine nucleotide translocator

FEBS Lett. 2012 Sep 21;586(19):3142-9. doi: 10.1016/j.febslet.2012.08.015. Epub 2012 Aug 23.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Apoptosis / physiology*
  • Cell Line, Tumor
  • Humans
  • Membrane Potential, Mitochondrial
  • Mitochondria / metabolism
  • Mitochondrial ADP, ATP Translocases / metabolism*
  • Mitochondrial Membrane Transport Proteins / metabolism
  • Mitochondrial Permeability Transition Pore
  • Mutagenesis, Site-Directed
  • Protein Interaction Domains and Motifs
  • Proto-Oncogene Proteins c-bcl-2 / chemistry
  • Proto-Oncogene Proteins c-bcl-2 / genetics
  • Proto-Oncogene Proteins c-bcl-2 / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Signal Transduction
  • Transfection

Substances

  • BCL2L13 protein, human
  • Mitochondrial Membrane Transport Proteins
  • Mitochondrial Permeability Transition Pore
  • Proto-Oncogene Proteins c-bcl-2
  • Recombinant Proteins
  • Adenosine Diphosphate
  • Mitochondrial ADP, ATP Translocases