期刊
MOLECULAR CELL
卷 52, 期 2, 页码 272-285出版社
CELL PRESS
DOI: 10.1016/j.molcel.2013.08.026
关键词
-
资金
- NNF-CPR
- Lundbeck Foundation
- European Union [262067]
- EURAtrans [HEALTH-F4-2010-241504]
- Swiss National Science Foundation [310030B_138667]
- Kanton of Zurich
- Swiss National Science Foundation (SNF) [310030B_138667] Funding Source: Swiss National Science Foundation (SNF)
- Novo Nordisk Foundation Center for Protein Research [PI Jiri Lukas, PI Michael Lund Nielsen] Funding Source: researchfish
Poly(ADP-ribos)ylation (PARylation) is a reversible posttranslational modification found in higher eukaryotes. However, little is known about PARylation acceptor proteins. Here, we describe a sensitive proteomics approach based on high-accuracy quantitative mass spectrometry for the identification of PARylated proteins induced under different cellular stress conditions. While confirming the majority of known PARylated substrates, our screen identifies numerous additional PARylation targets. In vivo and in vitro validation of acceptor proteins confirms that our methodology targets covalent PARylation. Nuclear proteins encompassing nucleic acid binding properties are prominently PARylated upon genotoxic stress, consistent with the nuclear localization of ARTD1/PARP1 and ARTD2/PARP2. Distinct differences in proteins becoming PARylated upon various genotoxic insults are observed, exemplified by the PARylation of RNA-processing factors THRAP3 and TAF15 under oxidative stress. High-content imaging reveals that PARylation affects the nuclear relocalization of THRAP3 and TAF15, demonstrating the potential of our approach to uncover hitherto unappreciated processes being controlled by specific genotoxic-stress-induced PARylation.
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