ADP‐ribosyltransferases, an update on function and nomenclature

ORCID
0000-0002-9622-8709
Affiliation
Institute of Biochemistry and Molecular Biology RWTH Aachen University Germany
Lüscher, Bernhard;
ORCID
0000-0002-9446-3756
Affiliation
Sir William Dunn School of Pathology University of Oxford UK
Ahel, Ivan;
Affiliation
Department of Molecular Mechanisms of Disease University of Zurich Switzerland
Altmeyer, Matthias;
Affiliation
UCSF Helen Diller Family Comprehensive Cancer Center San Francisco CA USA
Ashworth, Alan;
Affiliation
Department of Medical Chemistry Faculty of Medicine University of Debrecen Hungary
Bai, Peter;
Affiliation
ARase Therapeutics Cambridge MA USA
Chang, Paul;
Affiliation
Department of Chemical Physiology and Biochemistry Oregon Health and Science University Portland OR USA
Cohen, Michael;
Affiliation
Department of Biomedical Sciences National Research Council Rome Italy
Corda, Daniela;
Affiliation
CNRS, BSC‐UMR7242 Illkirch France
Dantzer, Françoise;
Affiliation
Division of Biological Sciences University of California San Diego La Jolla CA USA
Daugherty, Matthew D.;
Affiliation
Neuroregeneration and Stem Cell Programs Institute for Cell Engineering Johns Hopkins University School of Medicine Baltimore MD USA
Dawson, Ted M.;
Affiliation
Neuroregeneration and Stem Cell Programs Institute for Cell Engineering Johns Hopkins University School of Medicine Baltimore MD USA
Dawson, Valina L.;
Affiliation
Department of Cell and Molecular Biology Uppsala University Sweden
Deindl, Sebastian;
Affiliation
Department of Molecular Biosciences The University of Kansas Lawrence KS USA
Fehr, Anthony R.;
Affiliation
Institute of Biochemistry and Molecular Biology RWTH Aachen University Germany
Feijs, Karla L. H.;
Affiliation
Leiden Institute of Chemistry Leiden University The Netherlands
Filippov, Dmitri V.;
Affiliation
Department of Molecular Biology, Medical Biochemistry and Pathology Faculty of Medicine Laval University Quebec City QC Canada
Gagné, Jean‐Philippe;
Affiliation
National Research Council Naples Italy
Grimaldi, Giovanna;
Affiliation
Divisions of Structural Biology and Cancer Biology The Institute of Cancer Research (ICR) London UK
Guettler, Sebastian;
Affiliation
Department of Biochemistry University of São Paulo Brazil
Hoch, Nicolas C.;
Affiliation
Department of Molecular Mechanisms of Disease University of Zurich Switzerland
Hottiger, Michael O.;
Affiliation
Institute of Biochemistry and Molecular Biology RWTH Aachen University Germany
Korn, Patricia;
Affiliation
Cecil H. and Ida Green Center for Reproductive Biology Sciences University of Texas Southwestern Medical Center Dallas TX USA
Kraus, W. Lee;
Affiliation
Department of Physiological Chemistry Ludwig‐Maximilians‐University of Munich Planegg‐Martinsried Germany
Ladurner, Andreas;
Affiliation
Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu University of Oulu Finland
Lehtiö, Lari;
Affiliation
Department of Biochemistry and Molecular Biology Bloomberg School of Public Health Johns Hopkins University Baltimore MD USA
Leung, Anthony K. L.;
Affiliation
CRUK Gene Function Laboratory The Breast Cancer Now Toby Robins Research Centre The Institute of Cancer Research London UK
Lord, Christopher J.;
Affiliation
Department of Biology University of Konstanz Germany
Mangerich, Aswin;
Affiliation
Max Planck Institute for Biology of Ageing Cologne Germany
Matic, Ivan;
Affiliation
Institute of Basic Medical Sciences University of Oslo Norway
Matthews, Jason;
Affiliation
Department of Biochemistry and Molecular Biology The Pennsylvania State University College of Medicine Hershey PA USA
Moldovan, George‐Lucian;
Affiliation
National Heart, Lung, and Blood Institute National Institutes of Health Bethesda MD USA
Moss, Joel;
Affiliation
Department of Experimental Oncology European Institute of Oncology (IEO) Milan Italy
Natoli, Gioacchino;
Affiliation
Proteomics Program Novo Nordisk Foundation Center for Protein Research Faculty of Health and Medical Sciences University of Copenhagen Denmark
Nielsen, Michael L.;
ORCID
0000-0003-1415-6295
Affiliation
Ribon Therapeutics Cambridge MA USA
Niepel, Mario;
Affiliation
Institut für Immunologie Universitätsklinikum Hamburg‐Eppendorf Germany
Nolte, Friedrich;
Affiliation
Biochemistry and Molecular Medicine Université de Montréal Canada
Pascal, John;
Affiliation
Department of Biochemistry and Molecular Genetics University of Virginia Charlottesville VA USA
Paschal, Bryce M.;
Affiliation
Department of Molecular Biology University of Texas Southwestern Medical Center Dallas TX USA
Pawłowski, Krzysztof;
Affiliation
Department of Molecular Biology, Medical Biochemistry and Pathology Faculty of Medicine Laval University Quebec City QC Canada
Poirier, Guy G.;
Affiliation
Department of Pathology Kimmel Center for Biology and Medicine at the Skirball Institute New York University School of Medicine NY USA
Smith, Susan;
Affiliation
Lendület Laboratory of DNA Damage and Nuclear Dynamics Institute of Genetics Biological Research Centre Eötvös Loránd Research Network (ELKH) Szeged Hungary
Timinszky, Gyula;
GND
1216659737
Affiliation
Leibniz Institute on Aging – Fritz Lipmann Institute (FLI) Jena
Wang, Zhao‐Qi;
Affiliation
Cancer Research Program Hospital del Mar Medical Research Institute (IMIM) Barcelona Spain
Yélamos, José;
Affiliation
School of Life Sciences Westlake University Hangzhou China
Yu, Xiaochun;
Affiliation
Institute of Biochemistry and Molecular Biology RWTH Aachen University Germany
Zaja, Roko;
Affiliation
Department of Biomedicine University of Bergen Norway
Ziegler, Mathias

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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