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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 RIS Download

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

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