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

Citation
N. Ke et al., Bcl-B, a novel Bcl-2 family member that differentially binds and regulatesBax and Bak, J BIOL CHEM, 276(16), 2001, pp. 12481-12484
Citations number
17
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
00219258 → ACNP
Volume
276
Issue
16
Year of publication
2001
Pages
12481 - 12484
Database
ISI
SICI code
0021-9258(20010420)276:16<12481:BANBFM>2.0.ZU;2-T
Abstract
A novel human member of the Bcl-2 family was identified, Bcl-B, which is cl osest 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 Bar but not Bah. In transient transfection assays, Bcl-B suppress es apoptosis induced by Bar but not Bah. Deletion of the TM domain of Bcl-B impairs its association with intracellular organelles and diminishes its a nti-apoptotic function. Bcl-B thus displays a unique pattern of selectivity for binding and regulating the function of other members of the Bcl-2 fami ly.