THE ONCOPROTEIN BCL-3 DIRECTLY TRANSACTIVATES THROUGH KAPPA-B MOTIFS VIA ASSOCIATION WITH DNA-BINDING P50B HOMODIMERS

被引：409

作者：

BOURS, V ^{[1
]}

FRANZOSO, G ^{[1
]}

AZARENKO, V ^{[1
]}

PARK, S ^{[1
]}

KANNO, T ^{[1
]}

BROWN, K ^{[1
]}

SIEBENLIST, U ^{[1
]}

机构：

[1] NIAID,IMMUNOREGULAT LAB,BETHESDA,MD 20892

来源：

CELL | 1993年 / 72卷 / 05期

关键词：

D O I：

10.1016/0092-8674(93)90401-B

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：

Bcl-3 is an IkappaB-related protein with ankyrin repeat motifs. Its gene is located at a site of recurrent translocations in a subset of B cell chronic lymphocytic leukemias. Bcl-3 associates tightly with p50B (NFKB2, p52) homodimers in cells, and together these proteins form a ternary complex with DNA at kappaB sites. Such an association functionally leads to a novel and potent form of transactivation through the kappaB motif: the tethering of Bcl-3 to DNA via the p50B homodimers allows Bcl-3 to transactivate directly, while p50B homodimers alone cannot. Transactivation mediated by Bcl-3 requires two cooperating domains located amino- and carboxy-terminal to the ankyrin domain. Bcl-3 is localized to the nucleus, and a Bcl-3-p50B complex is detected in certain lymphoid cells. Our data reveal a novel role for Bcl-3, distinct from that of the inhibitor IkappaB. The results have implications for tumorigenesis.

引用

页码：729 / 739

页数：11

共 79 条

[1] THE INDUCIBLE TRANSCRIPTION ACTIVATOR NF-KAPPA-B - REGULATION BY DISTINCT PROTEIN SUBUNITS [J].