Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 276, Issue 16, Pages 12481-12484Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C000871200
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- NIGMS NIH HHS [GM-60554] Funding Source: Medline
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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 Bah. In transient transfection assays, Bcl-B suppresses apoptosis induced by Bax but not Bah. 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.
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