University of Oulu

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., Hoch, N.C., Hottiger, M.O., Korn, P., Kraus, W.L., Ladurner, A., Lehtiö, L., Leung, A.K.L., Lord, C.J., Mangerich, A., Matic, I., Matthews, J., Moldovan, G.-L., Moss, J., Natoli, G., Nielsen, M.L., Niepel, M., Nolte, F., Pascal, J., Paschal, B.M., Pawłowski, K., Poirier, G.G., Smith, S., Timinszky, G., Wang, Z.-Q., Yélamos, J., Yu, X., Zaja, R. and Ziegler, M. (2021), ADP-ribosyltransferases, an update on function and nomenclature. FEBS J. https://doi.org/10.1111/febs.16142

ADP-ribosyltransferases, an update on function and nomenclature

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Author: Lüscher, Bernhard1; Ahel, Ivan2; Altmeyer, Matthias3;
Organizations: 1Institute of Biochemistry and Molecular Biology, RWTH Aachen University, Germany
2Sir William Dunn School of Pathology, University of Oxford, UK
3Department of Molecular Mechanisms of Disease, University of Zurich, Switzerland
4UCSF Helen Diller Family Comprehensive Cancer Center, San Francisco, CA, USA
5Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, Hungary
6ARase Therapeutics, Cambridge, MA, USA
7Department of Chemical Physiology and Biochemistry, Oregon Health and Science University, Portland, OR, USA
8Department of Biomedical Sciences, National Research Council, Rome, Italy
9CNRS, BSC-UMR7242, Illkirch, France
10Division of Biological Sciences, University of California San Diego, La Jolla, CA, USA
11Neuroregeneration and Stem Cell Programs, Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD, USA
12Department of Cell and Molecular Biology, Uppsala University, Sweden
13Department of Molecular Biosciences, The University of Kansas, Lawrence, KS, USA
14Leiden Institute of Chemistry, Leiden University, The Netherlands
15Department of Molecular Biology, Medical Biochemistry and Pathology, Faculty of Medicine, Laval University, Quebec City, QC, Canada
16National Research Council, Naples, Italy
17Divisions of Structural Biology and Cancer Biology, The Institute of Cancer Research (ICR), London, UK
18Department of Biochemistry, University of São Paulo, Brazil
19Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, TX, USA
20Department of Physiological Chemistry, Ludwig-Maximilians-University of Munich, Planegg-Martinsried, Germany
21Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Finland
22Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD, USA
23CRUK Gene Function Laboratory, The Breast Cancer Now Toby Robins Research Centre, The Institute of Cancer Research, London, UK
24Department of Biology, University of Konstanz, Germany
25Max Planck Institute for Biology of Ageing, Cologne, Germany
26Cologne Excellence Cluster for Stress Responses in Ageing-Associated Diseases (CECAD), University of Cologne, Germany
27Institute of Basic Medical Sciences, University of Oslo, Norway
28Department of Biochemistry and Molecular Biology, The Pennsylvania State University College of Medicine, Hershey, PA, USA
29National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA
30Department of Experimental Oncology, European Institute of Oncology (IEO), Milan, Italy
31Proteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Denmark
32Ribon Therapeutics, Cambridge, MA, USA
33Institut für Immunologie, Universitätsklinikum Hamburg-Eppendorf, Germany
34Biochemistry and Molecular Medicine, Université de Montréal, Canada
35Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA
36Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA
37Department of Pathology, Kimmel Center for Biology and Medicine at the Skirball Institute, New York University School of Medicine, NY, USA
38Lendület Laboratory of DNA Damage and Nuclear Dynamics, Institute of Genetics, Biological Research Centre, Eötvös Loránd Research Network (ELKH), Szeged, Hungary
39Leibniz Institute on Aging – Fritz Lipmann Institute (FLI), Jena, Germany
40Faculty of Biological Sciences, Friedrich-Schiller University of Jena, Germany
41Cancer Research Program, Hospital del Mar Medical Research Institute (IMIM), Barcelona, Spain
42School of Life Sciences, Westlake University, Hangzhou, China
43Department of Biomedicine, University of Bergen, Norway
Format: article
Version: published version
Access: open
Online Access: PDF Full Text (PDF, 1.1 MB)
Persistent link: http://urn.fi/urn:nbn:fi-fe2021122061797
Language: English
Published: John Wiley & Sons, 2021
Publish Date: 2021-12-20
Description:

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.

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Series: FEBS journal
ISSN: 1742-464X
ISSN-E: 1742-4658
ISSN-L: 1742-464X
Issue: Early access
DOI: 10.1111/febs.16142
OADOI: https://oadoi.org/10.1111/febs.16142
Type of Publication: A1 Journal article – refereed
Field of Science: 1182 Biochemistry, cell and molecular biology
Subjects:
Funding: Funding for open access charge was supported by the German Research Foundation (LU466/16-2) and by core funding of the Institute of Biochemistry and Molecular Biology of RWTH Aachen University. JM was supported by the Intramural Research Program, NIH/NHLBI.
Copyright information: © 2021 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivsLicense, which permits use anddistribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
  https://creativecommons.org/licenses/by-nc-nd/4.0/