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Bcl-2/E1B 19 kDa-interacting protein 3-like protein (Bnip3L) interacts with bcl-2/Bcl-xL and induces apoptosis by altering mitochondrial membrane permeability.

We have previously reported on cloning of the human gene encoding Bcl-2/adenovirus E1B 19 kDa-interacting protein 3-like protein (Bnip3L) and its growth inhibitory effect on cancer cells. Here we show that Bnip3L contains a motif similar to the BH3 domain which is conserved in Bcl-2 family proteins as well as containing a membrane-anchoring domain, and that Bnip3L interacts with Bcl-2 and Bcl-xL. Immunofluorescence microscopy revealed that Bnip3L was localized in the mitochondria, when in the presence of the membrane-anchoring domain. Transient expression of Bnip3L induced apoptosis of Rat-1 and HeLa cells and mutational analysis revealed that the BH3 domain and the membrane-anchoring domain were required for Bnip3L to induce cell death. Addition of recombinant Bnip3L to isolated mitochondria induced membrane potential loss and cytochrome c release both of which have been suggested to be prerequisite for apoptotic cell death. These results suggest that Bnip3L is one of the BH3-containing pro-apoptotic proteins and that it targets the mitochondria when inducing apoptosis.

Pubmed ID: 10467396


  • Imazu T
  • Shimizu S
  • Tagami S
  • Matsushima M
  • Nakamura Y
  • Miki T
  • Okuyama A
  • Tsujimoto Y



Publication Data

August 12, 1999

Associated Grants


Mesh Terms

  • Adenovirus E1B Proteins
  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • Binding Sites
  • COS Cells
  • Cattle
  • Cell Line
  • HeLa Cells
  • Humans
  • Intracellular Membranes
  • Membrane Proteins
  • Mitochondria
  • Molecular Sequence Data
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • Rabbits
  • Rats
  • Sequence Homology, Amino Acid
  • Tumor Suppressor Proteins
  • bcl-X Protein