Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak
Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak
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DOI：
10.1074/jbc.c000871200
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发表时间：
2001-04-20
影响因子：
4.8
通讯作者：
Reed, JC
中科院分区：
文献类型：
--
作者：
Ke, N;Godzik, A;Reed, JC
Bcl-2家族的一个新的人类成员被鉴定为Bcl-B，其在氨基酸序列同源性上与Boo（Diva）蛋白最接近。Bcl-B蛋白含有四个Bcl-2同源（BH）结构域（BH 1、BH 2、BH 3、BH 4）和一个预测的羧基末端跨膜（TM）结构域。BCL-B mRNA在成人组织中广泛表达。Bcl-B蛋白结合Bcl-2、Bcl-X-L和Bax，但不结合Bah。在瞬时转染实验中，Bcl-B抑制Bax诱导的细胞凋亡，但不抑制Bah。Bcl-B的TM结构域的缺失损害了其与细胞内细胞器的结合并降低了其抗凋亡功能。因此，Bcl-B显示出独特的选择性模式，用于结合和调节Bcl-2家族其他成员的功能。
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.