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Sci. Signal., 24 May 2011
Vol. 4, Issue 174, p. mr5
[DOI: 10.1126/scisignal.2001645]


Progress in the Function and Regulation of ADP-Ribosylation

Michael O. Hottiger1*, Mark Boothby2{dagger}, Friedrich Koch-Nolte3{dagger}, Bernhard Lüscher4{dagger}, Niall M. B. Martin5{dagger}, Ruth Plummer6{dagger}, Zhao-Qi Wang7,8{dagger}, and Mathias Ziegler9{dagger}

1 Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
2 Department of Microbiology and Immunology, Vanderbilt University School of Medicine, 1161 21st Avenue S, Nashville, TN 37232–2363, USA.
3 Institute of Immunology, University Medical Center Hamburg-Eppendorf, Martinistrasse 52, 20246 Hamburg, Germany.
4 Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University, Pauwelsstrasse 30, 52057 Aachen, Germany
5 MISSION Therapeutics Ltd, Meditrina, Babraham Research Campus, Cambridge CB22 3AT, UK.
6 Northern Institute for Cancer Research, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, UK.
7 Leibniz Institute for Age Research–Fritz Lipmann Institute (FLI), Beutenbergstrasse 11, 07745 Jena, Germany.
8 Faculty of Biology and Pharmacy, Friedrich-Schiller-University Jena, Beutenbergstrasse 11, 07745 Jena, Germany.
9 Department of Molecular Biology, University of Bergen, Thormøhlensgate 55, 5008 Bergen, Norway.

{dagger} These authors are in alphabetical order. All authors contributed equally to this work.

A report on the 18th International Conference on ADP-Ribosylation, Zurich, Switzerland, 18 to 21 August 2010.

Abstract: Adenosine 5'-diphosphate (ADP)–ribosylation is a protein posttranslational modification that is catalyzed by ADP-ribosyltransferases (ARTs), using nicotinamide adenine dinucleotide (NAD+) as a substrate. Mono-ribosylation can be extended into polymers of ADP-ribose (PAR). Poly(ADP-ribosyl)polymerase (PARP) 1, the best-characterized cellular enzyme catalyzing this process, is the prototypical member of a family of mono- and poly(ADP-ribosyl)transferases. The physiological consequences of ADP-ribosylation are inadequately understood. PARP2010, the 18th International Conference on ADP-Ribosylation, attracted scientists from all over the world to Zurich, Switzerland. Highlights from this meeting include promising clinical trials with PARP inhibitors and new insights into cell, structural, and developmental biology of ARTs and the (glyco)hydrolase proteins that catalyze de-ADP-ribosylation of mono- or poly-ADP-ribosylated proteins. Moreover, potential links to the NAD-dependent sirtuin family were explored on the basis of a shared dependence on cellular NAD+ concentrations and the relationship of ADP-ribosylation with intermediary metabolism and cellular energetics.

* Corresponding author. E-mail, hottiger{at}; telephone, +41-44-635 54 74; fax, +41-44-635 68 40

Citation: M. O. Hottiger, M. Boothby, F. Koch-Nolte, B. Lüscher, N. M. B. Martin, R. Plummer, Z.-Q. Wang, M. Ziegler, Progress in the Function and Regulation of ADP-Ribosylation. Sci. Signal. 4, mr5 (2011).

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