期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 287, 期 35, 页码 29610-29619出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112.379768
关键词
-
资金
- National Institutes of Health [GM068608, GM081840, GM093600, P41 RR011823]
- Leukemia and Lymphoma Society
Protein modification by SUMO and ubiquitin critically impacts genome stability via effectors that read their signals using SUMO interaction motifs or ubiquitin binding domains, respectively. A novel mixed SUMO and ubiquitin signal is generated by the SUMO-targeted ubiquitin ligase (STUbL), which ubiquitylates SUMO conjugates. Herein, we determine that the ubiquitin-selective segregase Cdc48-Ufd1-Npl4 also binds SUMO via aSUMOinteraction motif in Ufd1 and can thus act as a selective receptor for STUbL targets. Indeed, we define key cooperative DNA repair functions for Cdc48-Ufd1-Npl4 and STUbL, thereby revealing a new signaling mechanism involving dual recruitment by SUMO and ubiquitin for Cdc48-Ufd1-Npl4 functions in maintaining genome stability.
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