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Originally published In Press as doi:10.1074/jbc.C000871200 on February 21, 2001

J. Biol. Chem., Vol. 276, Issue 16, 12481-12484, April 20, 2001
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ACCELERATED PUBLICATION
Bcl-B, a Novel Bcl-2 Family Member That Differentially Binds and Regulates Bax and Bak*

Ning Ke, Adam Godzik, and John C. ReedDagger

From The Burnham Institute, La Jolla, California 92037

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.

* This work was supported by National Institutes of Health Grant GM-60554, by CaP-CURE, and by United States Army Medical Research and Materiel Command Grant DAMD17-99-1-9511).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF326964.

Dagger To whom correspondence should be addresses: The Burnham Inst., 10901 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-646-3140; Fax: 858-646-3194; E-mail: jreed@burnham.org.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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