ADP-ribosyltransferases, an update on function and nomenclature

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

Standard

ADP-ribosyltransferases, an update on function and nomenclature. / Lüscher, Bernhard; Ahel, Ivan; Altmeyer, Matthias; Ashworth, Alan; Bai, Peter; Chang, Paul; Cohen, Michael; Corda, Daniela; Dantzer, Françoise; Daugherty, Matthew D.; Dawson, Ted M.; Dawson, Valina L.; Deindl, Sebastian; Fehr, Anthony R.; Feijs, Karla L.H.; Filippov, Dmitri V.; Gagné, Jean Philippe; Grimaldi, Giovanna; Guettler, Sebastian; Hoch, Nicolas C.; Hottiger, Michael O.; Korn, Patricia; Kraus, W. Lee; Ladurner, Andreas; Lehtiö, Lari; Leung, Anthony K.L.; Lord, Christopher J.; Mangerich, Aswin; Matic, Ivan; Matthews, Jason; Moldovan, George Lucian; Moss, Joel; Natoli, Gioacchino; Nielsen, Michael L.; Niepel, Mario; Nolte, Friedrich; Pascal, John; Paschal, Bryce M.; Pawłowski, Krzysztof; Poirier, Guy G.; Smith, Susan; Timinszky, Gyula; Wang, Zhao Qi; Yélamos, José; Yu, Xiaochun; Zaja, Roko; Ziegler, Mathias.

In: FEBS Journal, Vol. 289, No. 23, 2022, p. 7399-7410.

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

Harvard

Lüscher, B, Ahel, I, Altmeyer, M, Ashworth, A, Bai, P, Chang, P, Cohen, M, Corda, D, Dantzer, F, Daugherty, MD, Dawson, TM, Dawson, VL, Deindl, S, Fehr, AR, Feijs, KLH, Filippov, DV, Gagné, JP, Grimaldi, G, Guettler, S, Hoch, NC, Hottiger, MO, Korn, P, Kraus, WL, Ladurner, A, Lehtiö, L, Leung, AKL, Lord, CJ, Mangerich, A, Matic, I, Matthews, J, Moldovan, GL, Moss, J, Natoli, G, Nielsen, ML, Niepel, M, Nolte, F, Pascal, J, Paschal, BM, Pawłowski, K, Poirier, GG, Smith, S, Timinszky, G, Wang, ZQ, Yélamos, J, Yu, X, Zaja, R & Ziegler, M 2022, 'ADP-ribosyltransferases, an update on function and nomenclature', FEBS Journal, vol. 289, no. 23, pp. 7399-7410. https://doi.org/10.1111/febs.16142

APA

Lüscher, B., Ahel, I., Altmeyer, M., Ashworth, A., Bai, P., Chang, P., Cohen, M., Corda, D., Dantzer, F., Daugherty, M. D., Dawson, T. M., Dawson, V. L., Deindl, S., Fehr, A. R., Feijs, K. L. H., Filippov, D. V., Gagné, J. P., Grimaldi, G., Guettler, S., ... Ziegler, M. (2022). ADP-ribosyltransferases, an update on function and nomenclature. FEBS Journal, 289(23), 7399-7410. https://doi.org/10.1111/febs.16142

Vancouver

Lüscher B, Ahel I, Altmeyer M, Ashworth A, Bai P, Chang P et al. ADP-ribosyltransferases, an update on function and nomenclature. FEBS Journal. 2022;289(23):7399-7410. https://doi.org/10.1111/febs.16142

Author

Lüscher, Bernhard ; Ahel, Ivan ; Altmeyer, Matthias ; Ashworth, Alan ; Bai, Peter ; Chang, Paul ; Cohen, Michael ; Corda, Daniela ; Dantzer, Françoise ; Daugherty, Matthew D. ; Dawson, Ted M. ; Dawson, Valina L. ; Deindl, Sebastian ; Fehr, Anthony R. ; Feijs, Karla L.H. ; Filippov, Dmitri V. ; Gagné, Jean Philippe ; Grimaldi, Giovanna ; Guettler, Sebastian ; Hoch, Nicolas C. ; Hottiger, Michael O. ; Korn, Patricia ; Kraus, W. Lee ; Ladurner, Andreas ; Lehtiö, Lari ; Leung, Anthony K.L. ; Lord, Christopher J. ; Mangerich, Aswin ; Matic, Ivan ; Matthews, Jason ; Moldovan, George Lucian ; Moss, Joel ; Natoli, Gioacchino ; Nielsen, Michael L. ; Niepel, Mario ; Nolte, Friedrich ; Pascal, John ; Paschal, Bryce M. ; Pawłowski, Krzysztof ; Poirier, Guy G. ; Smith, Susan ; Timinszky, Gyula ; Wang, Zhao Qi ; Yélamos, José ; Yu, Xiaochun ; Zaja, Roko ; Ziegler, Mathias. / ADP-ribosyltransferases, an update on function and nomenclature. In: FEBS Journal. 2022 ; Vol. 289, No. 23. pp. 7399-7410.

Bibtex

@article{71139ff342cb4e18b8a0700a84fb4e05,
title = "ADP-ribosyltransferases, an update on function and nomenclature",
abstract = "ADP-ribosylation, a modification of proteins, nucleic acids, and metabolites, confers broad functions, including roles in stress responses elicited, for example, by DNA damage and viral infection and is involved in intra- and extracellular signaling, chromatin and transcriptional regulation, protein biosynthesis, and cell death. ADP-ribosylation is catalyzed by ADP-ribosyltransferases (ARTs), which transfer ADP-ribose from NAD+ onto substrates. The modification, which occurs as mono- or poly-ADP-ribosylation, is reversible due to the action of different ADP-ribosylhydrolases. Importantly, inhibitors of ARTs are approved or are being developed for clinical use. Moreover, ADP-ribosylhydrolases are being assessed as therapeutic targets, foremost as antiviral drugs and for oncological indications. Due to the development of novel reagents and major technological advances that allow the study of ADP-ribosylation in unprecedented detail, an increasing number of cellular processes and pathways are being identified that are regulated by ADP-ribosylation. In addition, characterization of biochemical and structural aspects of the ARTs and their catalytic activities have expanded our understanding of this protein family. This increased knowledge requires that a common nomenclature be used to describe the relevant enzymes. Therefore, in this viewpoint, we propose an updated and broadly supported nomenclature for mammalian ARTs that will facilitate future discussions when addressing the biochemistry and biology of ADP-ribosylation. This is combined with a brief description of the main functions of mammalian ARTs to illustrate the increasing diversity of mono- and poly-ADP-ribose mediated cellular processes.",
keywords = "ADP-ribosylation, MARylation, PARP, PARylation, posttranslational modification",
author = "Bernhard L{\"u}scher and Ivan Ahel and Matthias Altmeyer and Alan Ashworth and Peter Bai and Paul Chang and Michael Cohen and Daniela Corda and Fran{\c c}oise Dantzer and Daugherty, {Matthew D.} and Dawson, {Ted M.} and Dawson, {Valina L.} and Sebastian Deindl and Fehr, {Anthony R.} and Feijs, {Karla L.H.} and Filippov, {Dmitri V.} and Gagn{\'e}, {Jean Philippe} and Giovanna Grimaldi and Sebastian Guettler and Hoch, {Nicolas C.} and Hottiger, {Michael O.} and Patricia Korn and Kraus, {W. Lee} and Andreas Ladurner and Lari Lehti{\"o} and Leung, {Anthony K.L.} and Lord, {Christopher J.} and Aswin Mangerich and Ivan Matic and Jason Matthews and Moldovan, {George Lucian} and Joel Moss and Gioacchino Natoli and Nielsen, {Michael L.} and Mario Niepel and Friedrich Nolte and John Pascal and Paschal, {Bryce M.} and Krzysztof Paw{\l}owski and Poirier, {Guy G.} and Susan Smith and Gyula Timinszky and Wang, {Zhao Qi} and Jos{\'e} Y{\'e}lamos and Xiaochun Yu and Roko Zaja and Mathias Ziegler",
note = "Publisher Copyright: {\textcopyright} 2021 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.",
year = "2022",
doi = "10.1111/febs.16142",
language = "English",
volume = "289",
pages = "7399--7410",
journal = "F E B S Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "23",

}

RIS

TY - JOUR

T1 - ADP-ribosyltransferases, an update on function and nomenclature

AU - Lüscher, Bernhard

AU - Ahel, Ivan

AU - Altmeyer, Matthias

AU - Ashworth, Alan

AU - Bai, Peter

AU - Chang, Paul

AU - Cohen, Michael

AU - Corda, Daniela

AU - Dantzer, Françoise

AU - Daugherty, Matthew D.

AU - Dawson, Ted M.

AU - Dawson, Valina L.

AU - Deindl, Sebastian

AU - Fehr, Anthony R.

AU - Feijs, Karla L.H.

AU - Filippov, Dmitri V.

AU - Gagné, Jean Philippe

AU - Grimaldi, Giovanna

AU - Guettler, Sebastian

AU - Hoch, Nicolas C.

AU - Hottiger, Michael O.

AU - Korn, Patricia

AU - Kraus, W. Lee

AU - Ladurner, Andreas

AU - Lehtiö, Lari

AU - Leung, Anthony K.L.

AU - Lord, Christopher J.

AU - Mangerich, Aswin

AU - Matic, Ivan

AU - Matthews, Jason

AU - Moldovan, George Lucian

AU - Moss, Joel

AU - Natoli, Gioacchino

AU - Nielsen, Michael L.

AU - Niepel, Mario

AU - Nolte, Friedrich

AU - Pascal, John

AU - Paschal, Bryce M.

AU - Pawłowski, Krzysztof

AU - Poirier, Guy G.

AU - Smith, Susan

AU - Timinszky, Gyula

AU - Wang, Zhao Qi

AU - Yélamos, José

AU - Yu, Xiaochun

AU - Zaja, Roko

AU - Ziegler, Mathias

N1 - Publisher Copyright: © 2021 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.

PY - 2022

Y1 - 2022

N2 - ADP-ribosylation, a modification of proteins, nucleic acids, and metabolites, confers broad functions, including roles in stress responses elicited, for example, by DNA damage and viral infection and is involved in intra- and extracellular signaling, chromatin and transcriptional regulation, protein biosynthesis, and cell death. ADP-ribosylation is catalyzed by ADP-ribosyltransferases (ARTs), which transfer ADP-ribose from NAD+ onto substrates. The modification, which occurs as mono- or poly-ADP-ribosylation, is reversible due to the action of different ADP-ribosylhydrolases. Importantly, inhibitors of ARTs are approved or are being developed for clinical use. Moreover, ADP-ribosylhydrolases are being assessed as therapeutic targets, foremost as antiviral drugs and for oncological indications. Due to the development of novel reagents and major technological advances that allow the study of ADP-ribosylation in unprecedented detail, an increasing number of cellular processes and pathways are being identified that are regulated by ADP-ribosylation. In addition, characterization of biochemical and structural aspects of the ARTs and their catalytic activities have expanded our understanding of this protein family. This increased knowledge requires that a common nomenclature be used to describe the relevant enzymes. Therefore, in this viewpoint, we propose an updated and broadly supported nomenclature for mammalian ARTs that will facilitate future discussions when addressing the biochemistry and biology of ADP-ribosylation. This is combined with a brief description of the main functions of mammalian ARTs to illustrate the increasing diversity of mono- and poly-ADP-ribose mediated cellular processes.

AB - ADP-ribosylation, a modification of proteins, nucleic acids, and metabolites, confers broad functions, including roles in stress responses elicited, for example, by DNA damage and viral infection and is involved in intra- and extracellular signaling, chromatin and transcriptional regulation, protein biosynthesis, and cell death. ADP-ribosylation is catalyzed by ADP-ribosyltransferases (ARTs), which transfer ADP-ribose from NAD+ onto substrates. The modification, which occurs as mono- or poly-ADP-ribosylation, is reversible due to the action of different ADP-ribosylhydrolases. Importantly, inhibitors of ARTs are approved or are being developed for clinical use. Moreover, ADP-ribosylhydrolases are being assessed as therapeutic targets, foremost as antiviral drugs and for oncological indications. Due to the development of novel reagents and major technological advances that allow the study of ADP-ribosylation in unprecedented detail, an increasing number of cellular processes and pathways are being identified that are regulated by ADP-ribosylation. In addition, characterization of biochemical and structural aspects of the ARTs and their catalytic activities have expanded our understanding of this protein family. This increased knowledge requires that a common nomenclature be used to describe the relevant enzymes. Therefore, in this viewpoint, we propose an updated and broadly supported nomenclature for mammalian ARTs that will facilitate future discussions when addressing the biochemistry and biology of ADP-ribosylation. This is combined with a brief description of the main functions of mammalian ARTs to illustrate the increasing diversity of mono- and poly-ADP-ribose mediated cellular processes.

KW - ADP-ribosylation

KW - MARylation

KW - PARP

KW - PARylation

KW - posttranslational modification

U2 - 10.1111/febs.16142

DO - 10.1111/febs.16142

M3 - Journal article

C2 - 34323016

AN - SCOPUS:85114715698

VL - 289

SP - 7399

EP - 7410

JO - F E B S Journal

JF - F E B S Journal

SN - 1742-464X

IS - 23

ER -

ID: 280173076