期刊
STRUCTURE
卷 20, 期 7, 页码 1141-1153出版社
CELL PRESS
DOI: 10.1016/j.str.2012.04.009
关键词
-
资金
- U.S. Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]
- Ontario Ministry of Health and Long Term Care
- Canadian Cancer Society
- CCSRI
- Samuel Waxman Cancer Research Foundation
The E3 ligases recruit substrate proteins for targeted ubiquitylation. Recent insights into the mechanisms of ubiquitylation demonstrate that E3 ligases can possess active regulatory properties beyond those of a simple assembly scaffold. Here, we describe the dimeric structure of the E3 ligase adaptor protein SPOP (speckle-type POZ protein) in complex with the N-terminal domain of Cul3 at 2.4 angstrom resolution. We find that SPOP forms large oligomers that can form heteromeric species with the closely related paralog SPOPL. In combination, SPOP and SPOPL (SPOP-like) form a molecular rheostat that can fine-tune E3 ubiquitin ligase activity by affecting the oligomeric state of the E3 complex. We propose that adaptor protein self-assembly provides a graded level of regulation of the SPOP/Cul3 E3 ligase toward its multiple protein substrates.
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