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    J Biol Chem. 2001 Apr 20;276(16):12481-4. Epub 2001 Feb 21.

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

    Ke N, Godzik A, Reed JC.

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    Burnham Institute, La Jolla, California 92037, USA.

    Abstract

    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.

    PMID:
    11278245
    [PubMed - indexed for MEDLINE]
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