期刊
CELL REPORTS
卷 24, 期 9, 页码 2493-+出版社
CELL PRESS
DOI: 10.1016/j.celrep.2018.07.083
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资金
- Novo Nordisk Foundation Center for Protein Research
- Novo Nordisk Foundation [NNF14CC0001, NNF13OC0006477]
- Danish Council for Independent Research [DFF 4002-00051, DFF 4183-00322A]
- European Molecular Biology Organization [ALTF 503-2016]
ADP-ribosylation (ADPr) is a reversible posttranslational modification involved in a range of cellular processes. Here, we report system-wide identification of serine ADPr in human cells upon oxidative stress. High-resolution mass spectrometry and unrestricted data processing confirm that serine residues are the major target of ADPr in HeLa cells. Proteome-wide analysis identifies 3,090 serine ADPr sites, with 97% of acceptor sites modulating more than 2-fold upon oxidative stress, while treatment with the poly (ADP-ribose) polymerase (PARP) inhibitor olaparib abrogates this induction. Serine ADPr predominantly targets nuclear proteins, while structural-predictive analyses reveal that serine ADPr preferentially targets disordered protein regions. The identified ADP-ribosylated serines significantly overlap with known phosphorylated serines, and large-scale phosphoproteomics analysis provides evidence for site-specific crosstalk between serine ADPr and phosphorylation. Collectively, we demonstrate that serine ADPr is a widespread modification and a major nuclear signaling response to oxidative stress, with a regulatory scope comparable to other extensive posttranslational modifications.
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