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

被引：100
|
作者：
Ke, N [1 ]
Godzik, A [1 ]
Reed, JC [1 ]
机构：
[1] Burnham Inst, La Jolla, CA 92037 USA
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 2001年 / 276卷 / 16期
关键词：
D O I：
10.1074/jbc.C000871200
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：12481 / 12484
页数：4
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