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Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak.

A novel human member of the Bcl-2 family was identified, Bcl-B, which is closest in amino acid sequence homology to the Boo (Diva) protein. The Bcl-B protein contains four Bcl-2 homology (BH) domains (BH1, BH2, BH3, BH4) and a predicted carboxyl-terminal transmembrane (TM) domain. The BCL-B mRNA is widely expressed in adult human tissues. The Bcl-B protein binds Bcl-2, Bcl-X(L), and Bax but not Bak. In transient transfection assays, Bcl-B suppresses apoptosis induced by Bax but not Bak. Deletion of the TM domain of Bcl-B impairs its association with intracellular organelles and diminishes its anti-apoptotic function. Bcl-B thus displays a unique pattern of selectivity for binding and regulating the function of other members of the Bcl-2 family.

Pubmed ID: 11278245

Authors

  • Ke N
  • Godzik A
  • Reed JC

Journal

The Journal of biological chemistry

Publication Data

April 20, 2001

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM-60554

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • Carrier Proteins
  • Cell Line
  • Cloning, Molecular
  • Expressed Sequence Tags
  • Humans
  • Membrane Proteins
  • Mice
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Open Reading Frames
  • Organelles
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • RNA, Messenger
  • Recombinant Proteins
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Alignment
  • Sequence Deletion
  • Sequence Homology, Amino Acid
  • Transcription, Genetic
  • Transfection
  • bcl-2 Homologous Antagonist-Killer Protein
  • bcl-2-Associated X Protein