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

Research output: Contribution to journalJournal articlepeer-review

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Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue. / Martello, Rita; Leutert, Mario; Jungmichel, Stephanie; Bilan, Vera; Larsen, Sara C; Young, Clifford; Hottiger, Michael O; Nielsen, Michael L.

In: Nature Communications, Vol. 7, 12917, 01.10.2016.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Martello, R, Leutert, M, Jungmichel, S, Bilan, V, Larsen, SC, Young, C, Hottiger, MO & Nielsen, ML 2016, 'Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue', Nature Communications, vol. 7, 12917. https://doi.org/10.1038/ncomms12917

APA

Martello, R., Leutert, M., Jungmichel, S., Bilan, V., Larsen, S. C., Young, C., Hottiger, M. O., & Nielsen, M. L. (2016). Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue. Nature Communications, 7, [12917]. https://doi.org/10.1038/ncomms12917

Vancouver

Martello R, Leutert M, Jungmichel S, Bilan V, Larsen SC, Young C et al. Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue. Nature Communications. 2016 Oct 1;7. 12917. https://doi.org/10.1038/ncomms12917

Author

Martello, Rita ; Leutert, Mario ; Jungmichel, Stephanie ; Bilan, Vera ; Larsen, Sara C ; Young, Clifford ; Hottiger, Michael O ; Nielsen, Michael L. / Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue. In: Nature Communications. 2016 ; Vol. 7.

Bibtex

@article{734694484e8c4433b216322ed7c4a4e0,
title = "Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue",
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.",
author = "Rita Martello and Mario Leutert and Stephanie Jungmichel and Vera Bilan and Larsen, {Sara C} and Clifford Young and Hottiger, {Michael O} and Nielsen, {Michael L}",
year = "2016",
month = oct,
day = "1",
doi = "10.1038/ncomms12917",
language = "English",
volume = "7",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue

AU - Martello, Rita

AU - Leutert, Mario

AU - Jungmichel, Stephanie

AU - Bilan, Vera

AU - Larsen, Sara C

AU - Young, Clifford

AU - Hottiger, Michael O

AU - Nielsen, Michael L

PY - 2016/10/1

Y1 - 2016/10/1

N2 - 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.

AB - 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.

U2 - 10.1038/ncomms12917

DO - 10.1038/ncomms12917

M3 - Journal article

C2 - 27686526

VL - 7

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 12917

ER -

ID: 166502833