ADP-ribosyltransferases, an update on function and nomenclature

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• dc.contributor.author Lüscher, Bernhard
• dc.contributor.author Yélamos López, José
• dc.contributor.author Ziegler, Mathias
• dc.date.accessioned 2022-07-12T06:18:36Z
• dc.date.available 2022-07-12T06:18:36Z
• dc.date.issued 2022
• dc.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.
• dc.format.mimetype application/pdf
• dc.identifier.citation Lüscher B, Ahel I, Altmeyer M, Ashworth A, Bai P, Chang P, et al. ADP-ribosyltransferases, an update on function and nomenclature. FEBS J. 2022 Dec;289(23):7399-7410. DOI: 10.1111/febs.16142
• dc.identifier.doi http://dx.doi.org/10.1111/febs.16142
• dc.identifier.issn 1742-464X
• dc.identifier.uri http://hdl.handle.net/10230/53719
• dc.language.iso eng
• dc.publisher Wiley
• dc.rights This is the peer reviewed version of the following article: Lüscher B, Ahel I, Altmeyer M, Ashworth A, Bai P, Chang P, et al. ADP-ribosyltransferases, an update on function and nomenclature. FEBS J. 2021 Jul 29:10.1111/febs.16142, which has been published in final form at http://dx.doi.org/10.1111/febs.16142. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.
• dc.rights.accessRights info:eu-repo/semantics/openAccess
• dc.subject.keyword ADP-ribosylation
• dc.subject.keyword MARylation
• dc.subject.keyword PARP
• dc.subject.keyword PARylation
• dc.subject.keyword Posttranslational modification
• dc.title ADP-ribosyltransferases, an update on function and nomenclature
• dc.type info:eu-repo/semantics/article
• dc.type.version info:eu-repo/semantics/acceptedVersion