期刊
MOLECULAR CELL
卷 7, 期 5, 页码 915-926出版社
CELL PRESS
DOI: 10.1016/S1097-2765(01)00242-8
关键词
-
资金
- NCI NIH HHS [CA-67329] Funding Source: Medline
Destruction of beta -catenin is regulated through phosphorylation-dependent interactions with the F box protein beta -TrCP. A novel pathway for beta -catenin degradation was discovered involving mammalian homologs of Drosophila Sina (Siah), which bind ubiquitin-conjugating enzymes, and Ebi, an F box protein that binds beta -catenin independent of the phosphorylation sites recognized by beta -TrCP. A series of protein interactions were identified in which Siah is physically linked to Ebi by association with a novel Sgt1 homolog SIP that binds Skp1, a central component of Skp1 -Cullin-F box complexes. Expression of Siah is induced by p53, revealing a way of linking genotoxic injury to destruction of beta -catenin, thus reducing activity of Tcf/LEF transcription factors and contributing to cell cycle arrest.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据