Luscher, Bernhard ORCID: 0000-0002-9622-8709, Ahel, Ivan, Altmeyer, Matthias, Ashworth, Alan, Bai, Peter, Chang, Paul, Cohen, Michael, Corda, Daniela, Dantzer, Francoise, Daugherty, Matthew D., Dawson, Ted M., Dawson, Valina L., Deindl, Sebastian, Fehr, Anthony R., Feijs, Karla L. H., Filippov, Dmitri V., Gagne, Jean-Philippe, Grimaldi, Giovanna, Guettler, Sebastian ORCID: 0000-0002-3135-1546, Hoch, Nicolas C., Hottiger, Michael O., Korn, Patricia, Kraus, W. Lee, Ladurner, Andreas, Lehtio, Lari, Leung, Anthony K. L., Lord, Christopher J., Mangerich, Aswin, Matic, Ivan ORCID: 0000-0003-0170-7991, Matthews, Jason, Moldovan, George-Lucian, Moss, Joel, Natoli, Gioacchino ORCID: 0000-0003-0711-2411, Nielsen, Michael L., Niepel, Mario ORCID: 0000-0003-1415-6295, Nolte, Friedrich, Pascal, John, Paschal, Bryce M., Pawlowski, Krzysztof ORCID: 0000-0002-5367-0935, Poirier, Guy G., Smith, Susan, Timinszky, Gyula, Wang, Zhao-Qi, Yelamos, Jose, Yu, Xiaochun, Zaja, Roko and Ziegler, Mathias ORCID: 0000-0001-6961-2396 . ADP-ribosyltransferases, an update on function and nomenclature. FEBS J.. HOBOKEN: WILEY. ISSN 1742-4658

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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.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Luscher, BernhardUNSPECIFIEDorcid.org/0000-0002-9622-8709UNSPECIFIED
Ahel, IvanUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Altmeyer, MatthiasUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Ashworth, AlanUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Bai, PeterUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Chang, PaulUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Cohen, MichaelUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Corda, DanielaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Dantzer, FrancoiseUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Daugherty, Matthew D.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Dawson, Ted M.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Dawson, Valina L.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Deindl, SebastianUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Fehr, Anthony R.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Feijs, Karla L. H.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Filippov, Dmitri V.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Gagne, Jean-PhilippeUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Grimaldi, GiovannaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Guettler, SebastianUNSPECIFIEDorcid.org/0000-0002-3135-1546UNSPECIFIED
Hoch, Nicolas C.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Hottiger, Michael O.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Korn, PatriciaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Kraus, W. LeeUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Ladurner, AndreasUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Lehtio, LariUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Leung, Anthony K. L.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Lord, Christopher J.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Mangerich, AswinUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Matic, IvanUNSPECIFIEDorcid.org/0000-0003-0170-7991UNSPECIFIED
Matthews, JasonUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Moldovan, George-LucianUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Moss, JoelUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Natoli, GioacchinoUNSPECIFIEDorcid.org/0000-0003-0711-2411UNSPECIFIED
Nielsen, Michael L.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Niepel, MarioUNSPECIFIEDorcid.org/0000-0003-1415-6295UNSPECIFIED
Nolte, FriedrichUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Pascal, JohnUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Paschal, Bryce M.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Pawlowski, KrzysztofUNSPECIFIEDorcid.org/0000-0002-5367-0935UNSPECIFIED
Poirier, Guy G.UNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Smith, SusanUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Timinszky, GyulaUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Wang, Zhao-QiUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Yelamos, JoseUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Yu, XiaochunUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Zaja, RokoUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Ziegler, MathiasUNSPECIFIEDorcid.org/0000-0001-6961-2396UNSPECIFIED
URN: urn:nbn:de:hbz:38-608034
DOI: 10.1111/febs.16142
Journal or Publication Title: FEBS J.
Publisher: WILEY
Place of Publication: HOBOKEN
ISSN: 1742-4658
Language: English
Faculty: Unspecified
Divisions: Unspecified
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
POLY(ADP-RIBOSE) POLYMERASE; RIBOSYLATION; TANKYRASE; DNA; MAINTENANCE; INHIBITORS; INSIGHTS; DESIGN; PARP-1; CELLSMultiple languages
Biochemistry & Molecular BiologyMultiple languages
URI: http://kups.ub.uni-koeln.de/id/eprint/60803

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