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Proteomic Characterization of the Heart and Skeletal Muscle Reveals Widespread Arginine ADP-Ribosylation by the ARTC1 Ectoenzyme

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Proteomic Characterization of the Heart and Skeletal Muscle Reveals Widespread Arginine ADP-Ribosylation by the ARTC1 Ectoenzyme. / Leutert, Mario; Menzel, Stephan; Braren, Rickmer; Rissiek, Björn; Hopp, Ann-Katrin; Nowak, Kathrin; Bisceglie, Lavinia; Gehrig, Peter; Li, Hui; Zolkiewska, Anna; Koch-Nolte, Friedrich; Hottiger, Michael O.

In: CELL REP, Vol. 24, No. 7, 14.08.2018, p. 1916-1929.e5.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Leutert, M, Menzel, S, Braren, R, Rissiek, B, Hopp, A-K, Nowak, K, Bisceglie, L, Gehrig, P, Li, H, Zolkiewska, A, Koch-Nolte, F & Hottiger, MO 2018, 'Proteomic Characterization of the Heart and Skeletal Muscle Reveals Widespread Arginine ADP-Ribosylation by the ARTC1 Ectoenzyme', CELL REP, vol. 24, no. 7, pp. 1916-1929.e5. https://doi.org/10.1016/j.celrep.2018.07.048

APA

Leutert, M., Menzel, S., Braren, R., Rissiek, B., Hopp, A-K., Nowak, K., Bisceglie, L., Gehrig, P., Li, H., Zolkiewska, A., Koch-Nolte, F., & Hottiger, M. O. (2018). Proteomic Characterization of the Heart and Skeletal Muscle Reveals Widespread Arginine ADP-Ribosylation by the ARTC1 Ectoenzyme. CELL REP, 24(7), 1916-1929.e5. https://doi.org/10.1016/j.celrep.2018.07.048

Vancouver

Leutert M, Menzel S, Braren R, Rissiek B, Hopp A-K, Nowak K et al. Proteomic Characterization of the Heart and Skeletal Muscle Reveals Widespread Arginine ADP-Ribosylation by the ARTC1 Ectoenzyme. CELL REP. 2018 Aug 14;24(7):1916-1929.e5. https://doi.org/10.1016/j.celrep.2018.07.048

Bibtex

@article{a1c84008661a43d8a896cc9087d39f6f,
title = "Proteomic Characterization of the Heart and Skeletal Muscle Reveals Widespread Arginine ADP-Ribosylation by the ARTC1 Ectoenzyme",
abstract = "The clostridium-like ecto-ADP-ribosyltransferase ARTC1 is expressed in a highly restricted manner in skeletal muscle and heart tissue. Although ARTC1 is well studied, the identification of ARTC1 targets in vivo and subsequent characterization of ARTC1-regulated cellular processes on the proteome level have been challenging and only a few ARTC1-ADP-ribosylated targets are known. Applying our recently developed mass spectrometry-based workflow to C2C12 myotubes and to skeletal muscle and heart tissues from wild-type mice, we identify hundreds of ARTC1-ADP-ribosylated proteins whose modifications are absent in the ADP-ribosylome of ARTC1-deficient mice. These proteins are ADP-ribosylated on arginine residues and mainly located on the cell surface or in the extracellular space. They are associated with signal transduction, transmembrane transport, and muscle function. Validation of hemopexin (HPX) as a ARTC1-target protein confirmed the functional importance of ARTC1-mediated extracellular arginine ADP-ribosylation at the systems level.",
keywords = "Journal Article",
author = "Mario Leutert and Stephan Menzel and Rickmer Braren and Bj{\"o}rn Rissiek and Ann-Katrin Hopp and Kathrin Nowak and Lavinia Bisceglie and Peter Gehrig and Hui Li and Anna Zolkiewska and Friedrich Koch-Nolte and Hottiger, {Michael O}",
note = "Copyright {\textcopyright} 2018 The Author(s). Published by Elsevier Inc. All rights reserved.",
year = "2018",
month = aug,
day = "14",
doi = "10.1016/j.celrep.2018.07.048",
language = "English",
volume = "24",
pages = "1916--1929.e5",
journal = "CELL REP",
issn = "2211-1247",
publisher = "Elsevier",
number = "7",

}

RIS

TY - JOUR

T1 - Proteomic Characterization of the Heart and Skeletal Muscle Reveals Widespread Arginine ADP-Ribosylation by the ARTC1 Ectoenzyme

AU - Leutert, Mario

AU - Menzel, Stephan

AU - Braren, Rickmer

AU - Rissiek, Björn

AU - Hopp, Ann-Katrin

AU - Nowak, Kathrin

AU - Bisceglie, Lavinia

AU - Gehrig, Peter

AU - Li, Hui

AU - Zolkiewska, Anna

AU - Koch-Nolte, Friedrich

AU - Hottiger, Michael O

N1 - Copyright © 2018 The Author(s). Published by Elsevier Inc. All rights reserved.

PY - 2018/8/14

Y1 - 2018/8/14

N2 - The clostridium-like ecto-ADP-ribosyltransferase ARTC1 is expressed in a highly restricted manner in skeletal muscle and heart tissue. Although ARTC1 is well studied, the identification of ARTC1 targets in vivo and subsequent characterization of ARTC1-regulated cellular processes on the proteome level have been challenging and only a few ARTC1-ADP-ribosylated targets are known. Applying our recently developed mass spectrometry-based workflow to C2C12 myotubes and to skeletal muscle and heart tissues from wild-type mice, we identify hundreds of ARTC1-ADP-ribosylated proteins whose modifications are absent in the ADP-ribosylome of ARTC1-deficient mice. These proteins are ADP-ribosylated on arginine residues and mainly located on the cell surface or in the extracellular space. They are associated with signal transduction, transmembrane transport, and muscle function. Validation of hemopexin (HPX) as a ARTC1-target protein confirmed the functional importance of ARTC1-mediated extracellular arginine ADP-ribosylation at the systems level.

AB - The clostridium-like ecto-ADP-ribosyltransferase ARTC1 is expressed in a highly restricted manner in skeletal muscle and heart tissue. Although ARTC1 is well studied, the identification of ARTC1 targets in vivo and subsequent characterization of ARTC1-regulated cellular processes on the proteome level have been challenging and only a few ARTC1-ADP-ribosylated targets are known. Applying our recently developed mass spectrometry-based workflow to C2C12 myotubes and to skeletal muscle and heart tissues from wild-type mice, we identify hundreds of ARTC1-ADP-ribosylated proteins whose modifications are absent in the ADP-ribosylome of ARTC1-deficient mice. These proteins are ADP-ribosylated on arginine residues and mainly located on the cell surface or in the extracellular space. They are associated with signal transduction, transmembrane transport, and muscle function. Validation of hemopexin (HPX) as a ARTC1-target protein confirmed the functional importance of ARTC1-mediated extracellular arginine ADP-ribosylation at the systems level.

KW - Journal Article

U2 - 10.1016/j.celrep.2018.07.048

DO - 10.1016/j.celrep.2018.07.048

M3 - SCORING: Journal article

C2 - 30110646

VL - 24

SP - 1916-1929.e5

JO - CELL REP

JF - CELL REP

SN - 2211-1247

IS - 7

ER -