期刊
NATURE COMMUNICATIONS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms12917
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资金
- Novo Nordisk Foundation Center for Protein Research
- Novo Nordisk Foundation [NNF14CC0001, NNF13OC0006477]
- Lundbeck Foundation [R171-2014-1496]
- Danish Council of Independent Research [DFF 4002-00051, DFF 4183-00322A]
- Kanton of Zurich
- University Research Priority Program (URPP) in Translational Cancer Biology at the University of Zurich
- Swiss National Science Foundation [310030B_138667]
- Novo Nordisk Fonden [NNF13OC0006477] Funding Source: researchfish
- Novo Nordisk Foundation Center for Protein Research [PI Michael Lund Nielsen] Funding Source: researchfish
Although protein ADP-ribosylation is involved in diverse biological processes, it has remained a challenge to identify ADP-ribose acceptor sites. Here, we present an experimental workflow for sensitive and unbiased analysis of endogenous ADP-ribosylation sites, capable of detecting more than 900 modification sites in mammalian cells and mouse liver. In cells, we demonstrate that Lys residues, besides Glu, Asp and Arg residues, are the dominant in vivo targets of ADP-ribosylation during oxidative stress. In normal liver tissue, we find Arg residues to be the predominant modification site. The cellular distribution and biological processes that involve ADP-ribosylated proteins are different in cultured cells and liver tissue, in the latter of which the majority of sites were found to be in cytosolic and mitochondrial protein networks primarily associated with metabolism. Collectively, we describe a robust methodology for the assessment of the role of ADP-ribosylation and ADP-ribosyltransferases in physiological and pathological states.
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