ADP‐ribosyltransferases, an update on function and nomenclature

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2022
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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. Wiley. 2022, 289(23), pp. 7399-7410. ISSN 1742-464X. eISSN 1742-4658. Available under: doi: 10.1111/febs.16142
Zusammenfassung

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.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
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ADP-ribosylation, MARylation, PARP, PARylation, posttranslational modification
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ISO 690LÜSCHER, Bernhard, Ivan AHEL, Matthias ALTMEYER, Alan ASHWORTH, Peter BAI, Paul CHANG, Michael COHEN, Daniela CORDA, Françoise DANTZER, Aswin MANGERICH, 2022. ADP‐ribosyltransferases, an update on function and nomenclature. In: The FEBS Journal. Wiley. 2022, 289(23), pp. 7399-7410. ISSN 1742-464X. eISSN 1742-4658. Available under: doi: 10.1111/febs.16142
BibTex
@article{Luscher2022ADPri-54458,
  year={2022},
  doi={10.1111/febs.16142},
  title={ADP‐ribosyltransferases, an update on function and nomenclature},
  number={23},
  volume={289},
  issn={1742-464X},
  journal={The FEBS Journal},
  pages={7399--7410},
  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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