ADP‐ribosyltransferases, an update on function and nomenclature
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...
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| Published in | The FEBS journal Vol. 289; no. 23; pp. 7399 - 7410 |
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| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Blackwell Publishing Ltd
01.12.2022
Wiley |
| Subjects | |
| Online Access | Get full text |
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| 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.
ADP‐ribosylation, the transfer of ADP‐ribose from NAD+ onto substrates, is catalyzed by proteins with an ADP‐ribosyltransferase (ART) domain. This fully reversible modification can occur as mono‐ or poly‐ADP‐ribosylation. Here, we propose an updated nomenclature for mammalian ARTs and provide a brief description of the main functions of these proteins to illustrate the increasing diversity of the cellular processes that are regulated by mono‐ and poly‐ADP‐ribosylation. |
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| AbstractList | 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.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. 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. 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. 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. 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. 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. ADP‐ribosylation, the transfer of ADP‐ribose from NAD+ onto substrates, is catalyzed by proteins with an ADP‐ribosyltransferase (ART) domain. This fully reversible modification can occur as mono‐ or poly‐ADP‐ribosylation. Here, we propose an updated nomenclature for mammalian ARTs and provide a brief description of the main functions of these proteins to illustrate the increasing diversity of the cellular processes that are regulated by mono‐ and poly‐ADP‐ribosylation. |
| Author | Timinszky, Gyula Yélamos, José Zaja, Roko Lüscher, Bernhard Dantzer, Françoise Hottiger, Michael O. Deindl, Sebastian Paschal, Bryce M. Daugherty, Matthew D. Ladurner, Andreas Lord, Christopher J. Ziegler, Mathias Matthews, Jason Pawłowski, Krzysztof Niepel, Mario Ashworth, Alan Gagné, Jean‐Philippe Grimaldi, Giovanna Mangerich, Aswin Leung, Anthony K. L. Guettler, Sebastian Pascal, John Dawson, Valina L. Cohen, Michael Hoch, Nicolas C. Smith, Susan Chang, Paul Korn, Patricia Natoli, Gioacchino Wang, Zhao‐Qi Moldovan, George‐Lucian Moss, Joel Yu, Xiaochun Bai, Peter Fehr, Anthony R. Kraus, W. Lee Dawson, Ted M. Feijs, Karla L. H. Filippov, Dmitri V. Lehtiö, Lari Matic, Ivan Ahel, Ivan Nolte, Friedrich Corda, Daniela Poirier, Guy G. Altmeyer, Matthias Nielsen, Michael L. |
| AuthorAffiliation | 8 Department of Biomedical Sciences, National Research Council, Rome, Italy 26 Cologne Excellence Cluster for Stress Responses in Ageing-Associated Diseases (CECAD), University of Cologne, Germany 3 Department of Molecular Mechanisms of Disease, University of Zurich, Switzerland 25 Max Planck Institute for Biology of Ageing, Cologne, Germany 15 Department of Molecular Biology, Medical Biochemistry and Pathology, Faculty of Medicine, Laval University, Quebec City, QC, Canada 23 CRUK Gene Function Laboratory, The Breast Cancer Now Toby Robins Research Centre, The Institute of Cancer Research, London, UK 21 Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Finland 22 Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD, USA 30 Department of Experimental Oncology, European Institute of Oncology (IEO), Milan, Italy 13 Department of Molecular Biosciences, The University of Kansas, Lawrence, KS, |
| AuthorAffiliation_xml | – name: 25 Max Planck Institute for Biology of Ageing, Cologne, Germany – name: 23 CRUK Gene Function Laboratory, The Breast Cancer Now Toby Robins Research Centre, The Institute of Cancer Research, London, UK – name: 13 Department of Molecular Biosciences, The University of Kansas, Lawrence, KS, USA – name: 31 Proteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Denmark – name: 41 Cancer Research Program, Hospital del Mar Medical Research Institute (IMIM), Barcelona, Spain – name: 6 ARase Therapeutics, Cambridge, MA, USA – name: 17 Divisions of Structural Biology and Cancer Biology, The Institute of Cancer Research (ICR), London, UK – name: 10 Division of Biological Sciences, University of California San Diego, La Jolla, CA, USA – name: 27 Institute of Basic Medical Sciences, University of Oslo, Norway – name: 33 Institut für Immunologie, Universitätsklinikum Hamburg-Eppendorf, Germany – name: 12 Department of Cell and Molecular Biology, Uppsala University, Sweden – name: 22 Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD, USA – name: 8 Department of Biomedical Sciences, National Research Council, Rome, Italy – name: 4 UCSF Helen Diller Family Comprehensive Cancer Center, San Francisco, CA, USA – name: 1 Institute of Biochemistry and Molecular Biology, RWTH Aachen University, Germany – name: 36 Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA – name: 32 Ribon Therapeutics, Cambridge, MA, USA – name: 28 Department of Biochemistry and Molecular Biology, The Pennsylvania State University College of Medicine, Hershey, PA, USA – name: 43 Department of Biomedicine, University of Bergen, Norway – name: 3 Department of Molecular Mechanisms of Disease, University of Zurich, Switzerland – name: 42 School of Life Sciences, Westlake University, Hangzhou, China – name: 16 National Research Council, Naples, Italy – name: 2 Sir William Dunn School of Pathology, University of Oxford, UK – name: 5 Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, Hungary – name: 11 Neuroregeneration and Stem Cell Programs, Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD, USA – name: 39 Leibniz Institute on Aging – Fritz Lipmann Institute (FLI), Jena, Germany – name: 7 Department of Chemical Physiology and Biochemistry, Oregon Health and Science University, Portland, OR, USA – name: 15 Department of Molecular Biology, Medical Biochemistry and Pathology, Faculty of Medicine, Laval University, Quebec City, QC, Canada – name: 37 Department of Pathology, Kimmel Center for Biology and Medicine at the Skirball Institute, New York University School of Medicine, NY, USA – name: 14 Leiden Institute of Chemistry, Leiden University, The Netherlands – name: 9 CNRS, BSC-UMR7242, Illkirch, France – name: 20 Department of Physiological Chemistry, Ludwig-Maximilians-University of Munich, Planegg-Martinsried, Germany – name: 29 National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA – name: 30 Department of Experimental Oncology, European Institute of Oncology (IEO), Milan, Italy – name: 26 Cologne Excellence Cluster for Stress Responses in Ageing-Associated Diseases (CECAD), University of Cologne, Germany – name: 38 Lendület Laboratory of DNA Damage and Nuclear Dynamics, Institute of Genetics, Biological Research Centre, Eötvös Loránd Reserach Network (ELKH), Szeged, Hungary – name: 40 Faculty of Biological Sciences, Friedrich-Schiller University of Jena, Germany – name: 19 Cecil H. and Ida Green Center for Reproductive Biology Sciences, University of Texas Southwestern Medical Center, Dallas, TX, USA – name: 21 Faculty of Biochemistry and Molecular Medicine & Biocenter Oulu, University of Oulu, Finland – name: 34 Biochemistry and Molecular Medicine, Université de Montréal, Canada – name: 24 Department of Biology, University of Konstanz, Germany – name: 18 Department of Biochemistry, University of São Paulo, Brazil – name: 35 Department of Biochemistry and Molecular Genetics, University of Virgina, Charlottesville, VA, USA |
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L. organization: Johns Hopkins University – sequence: 27 givenname: Christopher J. surname: Lord fullname: Lord, Christopher J. organization: The Institute of Cancer Research – sequence: 28 givenname: Aswin surname: Mangerich fullname: Mangerich, Aswin organization: University of Konstanz – sequence: 29 givenname: Ivan surname: Matic fullname: Matic, Ivan organization: University of Cologne – sequence: 30 givenname: Jason surname: Matthews fullname: Matthews, Jason organization: University of Oslo – sequence: 31 givenname: George‐Lucian surname: Moldovan fullname: Moldovan, George‐Lucian organization: The Pennsylvania State University College of Medicine – sequence: 32 givenname: Joel surname: Moss fullname: Moss, Joel organization: National Institutes of Health – sequence: 33 givenname: Gioacchino surname: Natoli fullname: Natoli, Gioacchino organization: European Institute of Oncology (IEO) – sequence: 34 givenname: Michael L. surname: Nielsen fullname: Nielsen, Michael L. organization: University of Copenhagen – sequence: 35 givenname: Mario orcidid: 0000-0003-1415-6295 surname: Niepel fullname: Niepel, Mario organization: Ribon Therapeutics – sequence: 36 givenname: Friedrich surname: Nolte fullname: Nolte, Friedrich organization: Universitätsklinikum Hamburg‐Eppendorf – sequence: 37 givenname: John surname: Pascal fullname: Pascal, John organization: Université de Montréal – sequence: 38 givenname: Bryce M. surname: Paschal fullname: Paschal, Bryce M. organization: University of Virginia – sequence: 39 givenname: Krzysztof surname: Pawłowski fullname: Pawłowski, Krzysztof organization: University of Texas Southwestern Medical Center – sequence: 40 givenname: Guy G. surname: Poirier fullname: Poirier, Guy G. organization: Laval University – sequence: 41 givenname: Susan surname: Smith fullname: Smith, Susan organization: New York University School of Medicine – sequence: 42 givenname: Gyula surname: Timinszky fullname: Timinszky, Gyula organization: Eötvös Loránd Research Network (ELKH) – sequence: 43 givenname: Zhao‐Qi surname: Wang fullname: Wang, Zhao‐Qi organization: Friedrich‐Schiller University of Jena – sequence: 44 givenname: José surname: Yélamos fullname: Yélamos, José organization: Hospital del Mar Medical Research Institute (IMIM) – sequence: 45 givenname: Xiaochun surname: Yu fullname: Yu, Xiaochun organization: Westlake University – sequence: 46 givenname: Roko surname: Zaja fullname: Zaja, Roko organization: RWTH Aachen University – sequence: 47 givenname: Mathias surname: Ziegler fullname: Ziegler, Mathias organization: University of Bergen |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/34323016$$D View this record in MEDLINE/PubMed https://hal.science/hal-03442510$$DView record in HAL https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-497477$$DView record from Swedish Publication Index |
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| Cites_doi | 10.1074/jbc.M114.630160 10.1038/nchembio.2568 10.1038/s41571-018-0055-6 10.1093/nar/gkv1383 10.1016/j.gde.2019.04.013 10.1146/annurev.bi.54.070185.000445 10.1016/j.chembiol.2021.02.010 10.1021/acsmedchemlett.8b00429 10.1093/nar/gkab136 10.1016/j.celrep.2020.108176 10.1016/j.tibs.2009.12.003 10.1074/jbc.M109.077834 10.1016/j.chembiol.2018.09.011 10.1111/febs.15518 10.7717/peerj.11051 10.3390/cells10020313 10.1111/imm.13332 10.1128/MMBR.00040-05 10.1038/s41598-017-14156-8 10.1074/jbc.270.7.3247 10.1016/j.tcb.2019.06.005 10.1038/s41467-019-08859-x 10.1016/j.bcp.2019.07.004 10.3390/cancers10120487 10.1158/0008-5472.CAN-13-1701 10.1101/gad.334284.119 10.1038/s41598-019-55240-5 10.1038/s41586-018-0750-6 10.1016/j.semcdb.2016.09.010 10.1016/j.molcel.2008.08.009 10.1016/j.bmcl.2017.04.089 10.1093/nar/gky995 10.1038/s41467-020-18761-6 10.1111/febs.12320 10.1038/s41589-019-0362-y 10.2174/0929867043455611 10.1038/s41598-020-69229-y 10.1007/s00726-010-0676-2 10.1146/annurev.bi.46.070177.000523 10.1146/annurev-biochem-060815-014935 10.1016/j.molcel.2015.06.012 10.1038/nrm3376 10.1016/j.semcdb.2016.09.009 10.1074/jbc.274.25.17860 10.1126/science.aaa7227 10.1016/j.molcel.2017.04.028 10.1111/bph.14038 10.1021/acs.chemrev.7b00122 10.1021/jasms.0c00040 10.1002/cbic.202100047 10.1126/science.282.5393.1484 10.1016/j.celrep.2018.07.048 10.7554/eLife.60480 10.1101/gad.334433.119 10.1101/gad.291518.116 10.3390/cells10030680 10.1126/sciadv.abc0418 10.1042/BST20180416 10.1371/journal.pone.0037352 10.1016/j.bmcl.2018.04.056 10.1038/ncomms5426 10.1007/s00018-019-03366-0 10.1074/mcp.TIR119.001315 10.1126/science.aam7344 10.1038/nbt.2121 10.1016/j.chembiol.2016.08.012 10.1101/gad.334631.119 |
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| References | 2006; 70 2017; 7 2021; 22 2021; 288 2019; 55 2019; 10 2018; 564 2019; 15 2015; 384 2019; 18 2008; 32 2020; 11 2015; 348 2020; 10 2013; 280 2012; 13 2017; 355 2019; 167 2017; 31 2020; 6 2014; 5 2021; 32 2015; 290 2016; 85 2019; 29 1985; 54 1998; 282 2016; 44 2021; 9 2021; 49 2017; 63 2015; 58 2018; 28 2019; 9 2010; 35 2017; 27 2017; 66 2010; 285 2020; 34 2017; 174 1977; 46 2020; 77 2020; 32 1995; 270 2012; 30 2018; 25 2018; 24 2004; 11 2021; 10 2021 2018; 118 2020 2019; 47 1999; 274 2011; 41 2016; 63 2014; 74 2012; 7 2018; 10 2018; 15 2018; 14 2016; 23 e_1_2_11_70_1 e_1_2_11_32_1 e_1_2_11_55_1 e_1_2_11_30_1 e_1_2_11_57_1 e_1_2_11_36_1 e_1_2_11_51_1 e_1_2_11_13_1 e_1_2_11_34_1 e_1_2_11_53_1 e_1_2_11_11_1 e_1_2_11_29_1 e_1_2_11_6_1 e_1_2_11_27_1 e_1_2_11_4_1 e_1_2_11_48_1 e_1_2_11_2_1 e_1_2_11_60_1 e_1_2_11_45_1 e_1_2_11_66_1 e_1_2_11_68_1 e_1_2_11_24_1 e_1_2_11_41_1 e_1_2_11_62_1 e_1_2_11_8_1 e_1_2_11_22_1 e_1_2_11_43_1 e_1_2_11_64_1 e_1_2_11_17_1 e_1_2_11_15_1 e_1_2_11_59_1 e_1_2_11_38_1 e_1_2_11_19_1 e_1_2_11_50_1 Aravind L (e_1_2_11_20_1) 2015; 384 e_1_2_11_10_1 e_1_2_11_31_1 e_1_2_11_56_1 e_1_2_11_58_1 e_1_2_11_14_1 e_1_2_11_35_1 e_1_2_11_52_1 e_1_2_11_12_1 e_1_2_11_33_1 e_1_2_11_54_1 e_1_2_11_7_1 e_1_2_11_28_1 e_1_2_11_5_1 e_1_2_11_26_1 Cardamone MD (e_1_2_11_47_1) 2020 e_1_2_11_3_1 e_1_2_11_49_1 e_1_2_11_61_1 e_1_2_11_21_1 e_1_2_11_44_1 e_1_2_11_67_1 e_1_2_11_46_1 e_1_2_11_69_1 e_1_2_11_25_1 e_1_2_11_40_1 e_1_2_11_63_1 e_1_2_11_9_1 e_1_2_11_23_1 e_1_2_11_42_1 e_1_2_11_65_1 e_1_2_11_18_1 e_1_2_11_16_1 e_1_2_11_37_1 e_1_2_11_39_1 |
| References_xml | – volume: 11 start-page: 857 year: 2004 end-page: 872 article-title: Ecto‐ADP‐ribosyltransferases (ARTs): emerging actors in cell communication and signaling publication-title: Curr Med Chem – volume: 24 start-page: 1916 year: 2018 end-page: 1929 article-title: Proteomic characterization of the heart and skeletal muscle reveals widespread arginine ADP‐ribosylation by the ARTC1 ectoenzyme publication-title: Cell Rep – volume: 13 start-page: 411 year: 2012 end-page: 424 article-title: New insights into the molecular and cellular functions of poly(ADP‐ribose) and PARPs publication-title: Nat Rev Mol Cell Biol – volume: 18 start-page: 1010 year: 2019 end-page: 1026 article-title: An advanced strategy for comprehensive profiling of ADP‐ribosylation sites using mass spectrometry‐based proteomics publication-title: Mol Cell Proteomics – volume: 118 start-page: 1092 year: 2018 end-page: 1136 article-title: ADP‐ribosylation, a multifaceted posttranslational modification involved in the control of cell physiology in health and disease publication-title: Chem Rev – year: 2020 article-title: ADP‐ribosylation of mitochondrial proteins is mediated by neuralized‐like protein 4 (NEURL4) publication-title: bioRxiv – volume: 34 start-page: 302 year: 2020 end-page: 320 article-title: PARPs and ADP‐ribosylation in RNA biology: from RNA expression and processing to protein translation and proteostasis publication-title: Genes Dev – year: 2021 article-title: ADP‐ribosylation in evasion, promotion and exacerbation of immune responses publication-title: Immunology – volume: 70 start-page: 789 year: 2006 end-page: 829 article-title: Nuclear ADP‐ribosylation reactions in mammalian cells: where are we today and where are we going? publication-title: Microbiol Mol Biol Rev – volume: 34 start-page: 263 year: 2020 end-page: 284 article-title: (ADP‐ribosyl)hydrolases: structure, function, and biology publication-title: Genes Dev – volume: 23 start-page: 1251 year: 2016 end-page: 1260 article-title: Small‐molecule chemical probe rescues cells from mono‐ADP‐ribosyltransferase ARTD10/PARP10‐induced apoptosis and sensitizes cancer cells to DNA damage publication-title: Cell Chem Biol – volume: 564 start-page: 278 year: 2018 end-page: 282 article-title: NP220 mediates silencing of unintegrated retroviral DNA publication-title: Nature – volume: 9 year: 2021 article-title: A novel predicted ADP‐ribosyltransferase‐like family conserved in eukaryotic evolution publication-title: PeerJ – volume: 54 start-page: 73 year: 1985 end-page: 100 article-title: ADP‐ribosylation publication-title: Annu Rev Biochem – volume: 355 start-page: 1152 year: 2017 end-page: 1158 article-title: PARP inhibitors: synthetic lethality in the clinic publication-title: Science – volume: 58 start-page: 911 year: 2015 end-page: 924 article-title: The promise of proteomics for the study of ADP‐ribosylation publication-title: Mol Cell – volume: 6 year: 2020 article-title: Structural insights into ADP‐ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases publication-title: Sci Adv – volume: 85 start-page: 431 year: 2016 end-page: 454 article-title: Macrodomains: structure, function, evolution, and catalytic activities publication-title: Annu Rev Biochem – volume: 270 start-page: 3247 year: 1995 end-page: 3254 article-title: Role of glutamic acid 988 of human poly‐ADP‐ribose polymerase in polymer formation. Evidence for active site similarities to the ADP‐ribosylating toxins publication-title: J Biol Chem – volume: 15 start-page: 564 year: 2018 end-page: 576 article-title: Synthetic lethal therapies for cancer: what's next after PARP inhibitors? publication-title: Nat Rev Clin Oncol – volume: 7 year: 2012 article-title: PARP16/ARTD15 is a novel endoplasmic‐reticulum‐associated mono‐ADP‐ribosyltransferase that interacts with, and modifies karyopherin‐ss1 publication-title: PLoS One – volume: 9 start-page: 19130 year: 2019 article-title: Fragment‐based screening identifies molecules targeting the substrate‐binding ankyrin repeat domains of tankyrase publication-title: Sci Rep – volume: 31 start-page: 101 year: 2017 end-page: 126 article-title: PARPs and ADP‐ribosylation: recent advances linking molecular functions to biological outcomes publication-title: Genes Dev – year: 2021 article-title: A potent and selective PARP14 inhibitor decreases protumor macrophage gene expression and elicits inflammatory responses in tumor explants publication-title: Cell Chem Biol – volume: 47 start-page: D427 year: 2019 end-page: D432 article-title: The Pfam protein families database in 2019 publication-title: Nucleic Acids Res – volume: 41 start-page: 257 year: 2011 end-page: 269 article-title: ADP‐ribosylation of arginine publication-title: Amino Acids – volume: 10 start-page: 487 year: 2018 article-title: Role of BRCA mutations in cancer treatment with poly(ADP‐ribose) polymerase (PARP) inhibitors publication-title: Cancers (Basel) – volume: 288 start-page: 2131 year: 2021 end-page: 2142 article-title: Progress and outlook in studying the substrate specificities of PARPs and related enzymes publication-title: FEBS J – volume: 66 start-page: 503 year: 2017 end-page: 516 article-title: Ubiquitin modification by the E3 ligase/ADP‐ribosyltransferase Dtx3L/Parp9 publication-title: Mol Cell – volume: 30 start-page: 283 year: 2012 end-page: 288 article-title: Family‐wide chemical profiling and structural analysis of PARP and tankyrase inhibitors publication-title: Nat Biotechnol – volume: 47 start-page: 357 year: 2019 end-page: 370 article-title: ADP‐ribosylation and intracellular traffic: an emerging role for PARP enzymes publication-title: Biochem Soc Trans – volume: 280 start-page: 3576 year: 2013 end-page: 3593 article-title: Tankyrases as drug targets publication-title: FEBS J – volume: 29 start-page: 740 year: 2019 end-page: 751 article-title: Defining and modulating ‘BRCAness’ publication-title: Trends Cell Biol – volume: 11 start-page: 4940 year: 2020 article-title: TASOR is a pseudo‐PARP that directs HUSH complex assembly and epigenetic transposon control publication-title: Nat Commun – volume: 46 start-page: 95 year: 1977 end-page: 116 article-title: Poly(ADP‐ribose) and ADP‐ribosylation of proteins publication-title: Annu Rev Biochem – volume: 74 start-page: 31 year: 2014 end-page: 37 article-title: Targeting PARP‐1 allosteric regulation offers therapeutic potential against cancer publication-title: Cancer Res – volume: 10 year: 2021 article-title: Chemical genetics and proteome‐wide site mapping reveal cysteine MARylation by PARP‐7 on immune‐relevant protein targets publication-title: Elife – volume: 77 start-page: 19 year: 2020 end-page: 33 article-title: Poly(ADP‐ribose) polymerase enzymes and the maintenance of genome integrity publication-title: Cell Mol Life Sci – volume: 167 start-page: 86 year: 2019 end-page: 96 article-title: Overview of the mammalian ADP‐ribosyl‐transferases clostridia toxin‐like (ARTCs) family publication-title: Biochem Pharmacol – volume: 34 start-page: 321 year: 2020 end-page: 340 article-title: The role of ADP‐ribose metabolism in metabolic regulation, adipose tissue differentiation, and metabolism publication-title: Genes Dev – volume: 285 start-page: 8054 year: 2010 end-page: 8060 article-title: PARP‐3 is a mono‐ADP‐ribosylase that activates PARP‐1 in the absence of DNA publication-title: J Biol Chem – volume: 274 start-page: 17860 year: 1999 end-page: 17868 article-title: PARP‐2, a novel mammalian DNA damage‐dependent poly(ADP‐ribose) polymerase publication-title: J Biol Chem – volume: 10 start-page: 313 year: 2021 article-title: MARTs and MARylation in the cytosol: biological functions, mechanisms of action, and therapeutic potential publication-title: Cells – volume: 290 start-page: 7336 year: 2015 end-page: 7344 article-title: Structural basis for lack of ADP‐ribosyltransferase activity in poly(ADP‐ribose) polymerase‐13/zinc finger antiviral protein publication-title: J Biol Chem – volume: 10 start-page: 680 year: 2021 article-title: Uncovering the invisible: mono‐ADP‐ribosylation moved into the spotlight publication-title: Cells – volume: 15 start-page: 937 year: 2019 end-page: 944 article-title: Development of targeted protein degradation therapeutics publication-title: Nat Chem Biol – volume: 35 start-page: 208 year: 2010 end-page: 219 article-title: Toward a unified nomenclature for mammalian ADP‐ribosyltransferases publication-title: Trends Biochem Sci – volume: 282 start-page: 1484 year: 1998 end-page: 1487 article-title: Tankyrase, a poly(ADP‐ribose) polymerase at human telomeres publication-title: Science – volume: 32 start-page: 57 year: 2008 end-page: 69 article-title: Substrate‐assisted catalysis by PARP10 limits its activity to mono‐ADP‐ribosylation publication-title: Mol Cell – volume: 55 start-page: 1 year: 2019 end-page: 10 article-title: Role of H3K9me3 heterochromatin in cell identity establishment and maintenance publication-title: Curr Opin Genet Dev – volume: 174 start-page: 4611 year: 2017 end-page: 4636 article-title: Regulation of Wnt/beta‐catenin signalling by tankyrase‐dependent poly(ADP‐ribosyl)ation and scaffolding publication-title: Br J Pharmacol – volume: 14 start-page: 236 year: 2018 end-page: 243 article-title: Insights into the biogenesis, function, and regulation of ADP‐ribosylation publication-title: Nat Chem Biol – volume: 63 start-page: 114 year: 2017 end-page: 122 article-title: Cell fate regulation by chromatin ADP‐ribosylation publication-title: Semin Cell Dev Biol – volume: 10 start-page: 1182 year: 2019 article-title: Emerging roles of eraser enzymes in the dynamic control of protein ADP‐ribosylation publication-title: Nat Commun – volume: 25 start-page: 1547 year: 2018 end-page: 1553 article-title: A potent and selective PARP11 inhibitor suggests coupling between cellular localization and catalytic activity publication-title: Cell Chem Biol – volume: 384 start-page: 3 year: 2015 end-page: 32 article-title: The natural history of ADP‐ribosyltransferases and the ADP‐ribosylation system publication-title: Curr Top Microbiol Immunol – volume: 28 start-page: 2050 year: 2018 end-page: 2054 article-title: Design, synthesis and evaluation of potent and selective inhibitors of mono‐(ADP‐ribosyl)transferases PARP10 and PARP14 publication-title: Bioorg Med Chem Lett – volume: 32 start-page: 157 year: 2021 end-page: 168 article-title: Gas‐phase fragmentation of ADP‐ribosylated peptides: arginine‐specific side‐chain losses and their implication in database searches publication-title: J Am Soc Mass Spectrom – volume: 348 start-page: 1481 year: 2015 end-page: 1485 article-title: GENE SILENCING. Epigenetic silencing by the HUSH complex mediates position‐effect variegation in human cells publication-title: Science – volume: 7 start-page: 14035 year: 2017 article-title: PARP1‐produced poly‐ADP‐ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions publication-title: Sci Rep – volume: 32 year: 2020 article-title: Mapping physiological ADP‐ribosylation using activated ion electron transfer dissociation publication-title: Cell Rep – volume: 63 start-page: 92 year: 2016 end-page: 101 article-title: Expanding functions of ADP‐ribosylation in the maintenance of genome integrity publication-title: Semin Cell Dev Biol – volume: 44 start-page: 993 year: 2016 end-page: 1006 article-title: Readers of poly(ADP‐ribose): designed to be fit for purpose publication-title: Nucleic Acids Res – volume: 27 start-page: 2907 year: 2017 end-page: 2911 article-title: Design and synthesis of potent inhibitors of the mono(ADP‐ribosyl)transferase, PARP14 publication-title: Bioorg Med Chem Lett – volume: 49 start-page: 3634 year: 2021 end-page: 3650 article-title: ADP‐ribosylation of RNA and DNA: from in vitro characterization to in vivo function publication-title: Nucleic Acids Res – volume: 10 start-page: 12357 year: 2020 article-title: A FRET‐based high‐throughput screening platform for the discovery of chemical probes targeting the scaffolding functions of human tankyrases publication-title: Sci Rep – volume: 10 start-page: 74 year: 2019 end-page: 79 article-title: Rational design of cell‐active inhibitors of PARP10 publication-title: ACS Med Chem Lett – volume: 22 start-page: 2107 year: 2021 end-page: 2110 article-title: Targeted degradation of PARP14 using a heterobifunctional small molecule publication-title: ChemBioChem – volume: 5 start-page: 4426 year: 2014 article-title: Family‐wide analysis of poly(ADP‐ribose) polymerase activity publication-title: Nat Commun – ident: e_1_2_11_39_1 doi: 10.1074/jbc.M114.630160 – ident: e_1_2_11_4_1 doi: 10.1038/nchembio.2568 – ident: e_1_2_11_55_1 doi: 10.1038/s41571-018-0055-6 – ident: e_1_2_11_13_1 doi: 10.1093/nar/gkv1383 – ident: e_1_2_11_46_1 doi: 10.1016/j.gde.2019.04.013 – ident: e_1_2_11_28_1 doi: 10.1146/annurev.bi.54.070185.000445 – ident: e_1_2_11_65_1 doi: 10.1016/j.chembiol.2021.02.010 – ident: e_1_2_11_61_1 doi: 10.1021/acsmedchemlett.8b00429 – ident: e_1_2_11_3_1 doi: 10.1093/nar/gkab136 – ident: e_1_2_11_40_1 doi: 10.1016/j.celrep.2020.108176 – ident: e_1_2_11_21_1 doi: 10.1016/j.tibs.2009.12.003 – ident: e_1_2_11_38_1 doi: 10.1074/jbc.M109.077834 – ident: e_1_2_11_63_1 doi: 10.1016/j.chembiol.2018.09.011 – ident: e_1_2_11_10_1 doi: 10.1111/febs.15518 – ident: e_1_2_11_19_1 doi: 10.7717/peerj.11051 – ident: e_1_2_11_9_1 doi: 10.3390/cells10020313 – ident: e_1_2_11_24_1 doi: 10.1111/imm.13332 – ident: e_1_2_11_29_1 doi: 10.1128/MMBR.00040-05 – ident: e_1_2_11_37_1 doi: 10.1038/s41598-017-14156-8 – ident: e_1_2_11_33_1 doi: 10.1074/jbc.270.7.3247 – ident: e_1_2_11_57_1 doi: 10.1016/j.tcb.2019.06.005 – ident: e_1_2_11_12_1 doi: 10.1038/s41467-019-08859-x – ident: e_1_2_11_23_1 doi: 10.1016/j.bcp.2019.07.004 – ident: e_1_2_11_54_1 doi: 10.3390/cancers10120487 – ident: e_1_2_11_68_1 doi: 10.1158/0008-5472.CAN-13-1701 – ident: e_1_2_11_6_1 doi: 10.1101/gad.334284.119 – ident: e_1_2_11_69_1 doi: 10.1038/s41598-019-55240-5 – ident: e_1_2_11_44_1 doi: 10.1038/s41586-018-0750-6 – ident: e_1_2_11_7_1 doi: 10.1016/j.semcdb.2016.09.010 – volume: 384 start-page: 3 year: 2015 ident: e_1_2_11_20_1 article-title: The natural history of ADP‐ribosyltransferases and the ADP‐ribosylation system publication-title: Curr Top Microbiol Immunol – ident: e_1_2_11_32_1 doi: 10.1016/j.molcel.2008.08.009 – ident: e_1_2_11_64_1 doi: 10.1016/j.bmcl.2017.04.089 – ident: e_1_2_11_18_1 doi: 10.1093/nar/gky995 – ident: e_1_2_11_45_1 doi: 10.1038/s41467-020-18761-6 – ident: e_1_2_11_58_1 doi: 10.1111/febs.12320 – ident: e_1_2_11_66_1 doi: 10.1038/s41589-019-0362-y – ident: e_1_2_11_25_1 doi: 10.2174/0929867043455611 – ident: e_1_2_11_70_1 doi: 10.1038/s41598-020-69229-y – ident: e_1_2_11_26_1 doi: 10.1007/s00726-010-0676-2 – year: 2020 ident: e_1_2_11_47_1 article-title: ADP‐ribosylation of mitochondrial proteins is mediated by neuralized‐like protein 4 (NEURL4) publication-title: bioRxiv – ident: e_1_2_11_27_1 doi: 10.1146/annurev.bi.46.070177.000523 – ident: e_1_2_11_15_1 doi: 10.1146/annurev-biochem-060815-014935 – ident: e_1_2_11_17_1 doi: 10.1016/j.molcel.2015.06.012 – ident: e_1_2_11_22_1 doi: 10.1038/nrm3376 – ident: e_1_2_11_42_1 doi: 10.1016/j.semcdb.2016.09.009 – ident: e_1_2_11_31_1 doi: 10.1074/jbc.274.25.17860 – ident: e_1_2_11_43_1 doi: 10.1126/science.aaa7227 – ident: e_1_2_11_48_1 doi: 10.1016/j.molcel.2017.04.028 – ident: e_1_2_11_59_1 doi: 10.1111/bph.14038 – ident: e_1_2_11_5_1 doi: 10.1021/acs.chemrev.7b00122 – ident: e_1_2_11_52_1 doi: 10.1021/jasms.0c00040 – ident: e_1_2_11_67_1 doi: 10.1002/cbic.202100047 – ident: e_1_2_11_30_1 doi: 10.1126/science.282.5393.1484 – ident: e_1_2_11_50_1 doi: 10.1016/j.celrep.2018.07.048 – ident: e_1_2_11_35_1 doi: 10.7554/eLife.60480 – ident: e_1_2_11_2_1 doi: 10.1101/gad.334433.119 – ident: e_1_2_11_14_1 doi: 10.1101/gad.291518.116 – ident: e_1_2_11_8_1 doi: 10.3390/cells10030680 – ident: e_1_2_11_49_1 doi: 10.1126/sciadv.abc0418 – ident: e_1_2_11_16_1 doi: 10.1042/BST20180416 – ident: e_1_2_11_36_1 doi: 10.1371/journal.pone.0037352 – ident: e_1_2_11_62_1 doi: 10.1016/j.bmcl.2018.04.056 – ident: e_1_2_11_34_1 doi: 10.1038/ncomms5426 – ident: e_1_2_11_41_1 doi: 10.1007/s00018-019-03366-0 – ident: e_1_2_11_51_1 doi: 10.1074/mcp.TIR119.001315 – ident: e_1_2_11_56_1 doi: 10.1126/science.aam7344 – ident: e_1_2_11_53_1 doi: 10.1038/nbt.2121 – ident: e_1_2_11_60_1 doi: 10.1016/j.chembiol.2016.08.012 – ident: e_1_2_11_11_1 doi: 10.1101/gad.334631.119 |
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| Title | ADP‐ribosyltransferases, an update on function and nomenclature |
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