ADP‐ribosyltransferases, an update on function and nomenclature

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Date
2021
Authors
Lüscher, Bernhard
Ahel, Ivan
Altmeyer, Matthias
Ashworth, Alan
Bai, Peter
Chang, Paul
Cohen, Michael
Corda, Daniela
Dantzer, Françoise
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The FEBS Journal ; 2021. - Wiley. - ISSN 1742-464X. - eISSN 1742-4658
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, 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 ADP-ribosyltransferases are approved or are being developed for clinical use. Moreover, ADP-ribosylhydrolases are being assessed as therapeutic targets, foremost as anti-viral 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 ADP-ribosyltransferases 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 ADP-ribosyltransferases 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 ADP-ribosyltransferases to illustrate the increasing diversity of mono- and poly-ADP-ribose mediated cellular processes.
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570 Biosciences, Biology
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ADP-ribosylation, MARylation, PARP, PARylation, posttranslational modification
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Cite This
ISO 690LÜSCHER, Bernhard, Ivan AHEL, Matthias ALTMEYER, Alan ASHWORTH, Peter BAI, Paul CHANG, Michael COHEN, Daniela CORDA, Françoise DANTZER, Aswin MANGERICH, 2021. ADP‐ribosyltransferases, an update on function and nomenclature. In: The FEBS Journal. Wiley. ISSN 1742-464X. eISSN 1742-4658. Available under: doi: 10.1111/febs.16142
BibTex
@article{Luscher2021ADPri-54458,
  year={2021},
  doi={10.1111/febs.16142},
  title={ADP‐ribosyltransferases, an update on function and nomenclature},
  issn={1742-464X},
  journal={The FEBS Journal},
  author={Lüscher, Bernhard and Ahel, Ivan and Altmeyer, Matthias and Ashworth, Alan and Bai, Peter and Chang, Paul and Cohen, Michael and Corda, Daniela and Dantzer, Françoise and Mangerich, Aswin}
}
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