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Function and Regulation of the Mono-ADP-Ribosyltransferase ARTD10

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Endogenous ADP-Ribosylation

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 384))

Abstract

The transfer of ADP-ribose from NAD+ to a substrate by ADP-ribosyltransferases, ADP-ribosylation, is a multifunctional posttranslational modification. While many studies have addressed the function of poly-ADP-ribosylation, for example, in DNA repair, signaling, and gene transcription, little is known about the role of mono-ADP-ribosylation. Recent work describing the mono-ADP-ribosyltransferase ARTD10/PARP10 suggests that this enzyme affects apoptosis, NF-κB signaling, and DNA damage repair, at least in part dependent on its activity as mono-ADP-ribosyltransferase. Moreover, the macrodomain-containing proteins MacroD1, MacroD2, and TARG1/C6orf130 were recently described as hydrolases, which remove mono-ADP-ribosylation thus providing evidence that this modification is reversible. In this review, we discuss these novel findings and their broader implications for cell behavior. We suggest functions of ARTD10 in immunity, metabolism, and cancer biology.

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Abbreviations

ADAR:

Adenosine deaminases acting on RNA

APOB:

Apolipoprotein B

ARTC:

ADP-ribosyltransferases Cholera toxin-like

ARTD:

ADP-ribosyltransferase Diphtheria toxin-like

GSK3β:

Glycogen synthase kinase 3β

IFN:

Interferon

MEFs:

Mouse embryo fibroblasts

NES:

Nuclear export sequence

NLS:

Nuclear localization sequence

PIP:

PCNA-interacting peptide

PTM:

Posttranslational modification

RRM:

RNA recognition motif

SNP:

Single nucleotide polymorphism

UIM:

Ubiquitin interaction motif

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Acknowledgments

We thank Andrew Jefferson for editing the manuscript. The work in our laboratory was supported by a Mildred Scheel Stipend of the German Cancer Aid (to MK), the START program of the Medical School of the RWTH Aachen University, and by the Deutsche Forschungsgemeinschaft DFG (to BL).

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Authors and Affiliations

  1. Institute of Biochemistry and Molecular Biology, RWTH Aachen University, Pauwelsstraße 30, 52074, Aachen, Germany

    Max Kaufmann, Karla L. H. Feijs & Bernhard Lüscher

  2. Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX4 3TN, UK

    Karla L. H. Feijs

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  1. Max Kaufmann
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  2. Karla L. H. Feijs
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  3. Bernhard Lüscher
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Correspondence to Bernhard Lüscher .

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  1. Institute of Immunology, University Medical Center, Hamburg, Germany

    Friedrich Koch-Nolte

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Kaufmann, M., Feijs, K.L.H., Lüscher, B. (2014). Function and Regulation of the Mono-ADP-Ribosyltransferase ARTD10. In: Koch-Nolte, F. (eds) Endogenous ADP-Ribosylation. Current Topics in Microbiology and Immunology, vol 384. Springer, Cham. https://doi.org/10.1007/82_2014_379

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