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Papers In Press, published online ahead of print February 21, 2001
J. Biol. Chem, 10.1074/jbc.C000871200
Submitted on December 11, 2000
Revised on February 20, 2001
Accepted on February 21, 2001
The Burnham Institute, La Jolla, CA 92037
Corresponding Author: rcornell{at}burnham-inst.org
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-XL , 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.
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