Progress in the Function and Regulation of ADP-Ribosylation

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

  1. Michael O. Hottiger1,*,
  2. Mark Boothby2,,
  3. Friedrich Koch-Nolte3,,
  4. Bernhard Lüscher4,,
  5. Niall M. B. Martin5,,
  6. Ruth Plummer6,,
  7. Zhao-Qi Wang7,8,, and
  8. Mathias Ziegler9,
  1. 1Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
  2. 2Department of Microbiology and Immunology, Vanderbilt University School of Medicine, 1161 21st Avenue S, Nashville, TN 37232–2363, USA.
  3. 3Institute of Immunology, University Medical Center Hamburg-Eppendorf, Martinistrasse 52, 20246 Hamburg, Germany.
  4. 4Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University, Pauwelsstrasse 30, 52057 Aachen, Germany
  5. 5MISSION Therapeutics Ltd, Meditrina, Babraham Research Campus, Cambridge CB22 3AT, UK.
  6. 6Northern Institute for Cancer Research, Newcastle University, Framlington Place, Newcastle upon Tyne NE2 4HH, UK.
  7. 7Leibniz Institute for Age Research–Fritz Lipmann Institute (FLI), Beutenbergstrasse 11, 07745 Jena, Germany.
  8. 8Faculty of Biology and Pharmacy, Friedrich-Schiller-University Jena, Beutenbergstrasse 11, 07745 Jena, Germany.
  9. 9Department of Molecular Biology, University of Bergen, Thormøhlensgate 55, 5008 Bergen, Norway.
  1. *Corresponding author. E-mail, hottiger{at}vetbio.uzh.ch; telephone, +41-44-635 54 74; fax, +41-44-635 68 40
  • 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.

Citation:

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

Regulation of Mitochondrial Poly(ADP-Ribose) Polymerase Activation by the {beta}-Adrenoceptor/cAMP/Protein Kinase A Axis during Oxidative Stress
A. Brunyanszki, G. Olah, C. Coletta, B. Szczesny, and C. Szabo
Mol. Pharmacol. 86, 450-462 (1 October 2014)

ADP-ribosyltransferases Parp1 and Parp7 safeguard pluripotency of ES cells
S. J. Roper, S. Chrysanthou, C. E. Senner, A. Sienerth, S. Gnan, A. Murray, M. Masutani, P. Latos, and M. Hemberger
Nucleic Acids Res 42, 8914-8927 (18 August 2014)

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