Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue

Rita Martello, Mario Leutert, Stephanie Jungmichel, Vera Bilan, Sara C. Larsen, Clifford Young, Michael O. Hottiger and Michael L. Nielsen ()
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Rita Martello: Faculty of Health Sciences, The Novo Nordisk Foundation Centre for Protein Research, University of Copenhagen
Mario Leutert: University of Zurich
Stephanie Jungmichel: Faculty of Health Sciences, The Novo Nordisk Foundation Centre for Protein Research, University of Copenhagen
Vera Bilan: University of Zurich
Sara C. Larsen: Faculty of Health Sciences, The Novo Nordisk Foundation Centre for Protein Research, University of Copenhagen
Clifford Young: Faculty of Health Sciences, The Novo Nordisk Foundation Centre for Protein Research, University of Copenhagen
Michael O. Hottiger: University of Zurich
Michael L. Nielsen: Faculty of Health Sciences, The Novo Nordisk Foundation Centre for Protein Research, University of Copenhagen

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: Abstract 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.

Date: 2016
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DOI: 10.1038/ncomms12917

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