Nucleic Acids Research Advance Access originally published online on November 3, 2008
Nucleic Acids Research 2008 36(22):6959-6976; doi:10.1093/nar/gkn771
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Nucleic Acids Research, 2008, Vol. 36, No. 22 6959-6976
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Molecular Biology |
Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes
1Laval University Medical Research Center, CHUQ, Faculty of Medicine, Laval University, Québec, Canada G1V4G2, 2CNRS, UMR 6061, Institut de Génétique et Développement de Rennes, Université de Rennes 1, Rennes, France, 3Proteomics Platform, Québec Genomic Center, Laval University Medical Research Center, CHUQ, Faculty of Medicine, Laval University, Québec, Canada G1V4G2, 4Department of Oncology, University of Alberta and Cross Cancer Institute, Edmonton, Alberta, Canada T6G 1Z2 and 5Neuroregeneration and Stem Cell Programs, Institute for Cell Engineering, Department of Neurology and the Solomon H Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
*To whom correspondence should be addressed. Tel: +1 418 654 2267; Fax: +1 418 654 2159; Email: guy.poirier{at}crchul.ulaval.ca
Received July 17, 2008. Revised October 6, 2008. Accepted October 7, 2008.
Poly(ADP-ribose) (pADPr) is a polymer assembled from the enzymatic polymerization of the ADP-ribosyl moiety of NAD by poly(ADP-ribose) polymerases (PARPs). The dynamic turnover of pADPr within the cell is essential for a number of cellular processes including progression through the cell cycle, DNA repair and the maintenance of genomic integrity, and apoptosis. In spite of the considerable advances in the knowledge of the physiological conditions modulated by poly(ADP-ribosyl)ation reactions, and notwithstanding the fact that pADPr can play a role of mediator in a wide spectrum of biological processes, few pADPr binding proteins have been identified so far. In this study, refined in silico prediction of pADPr binding proteins and large-scale mass spectrometry-based proteome analysis of pADPr binding proteins were used to establish a comprehensive repertoire of pADPr-associated proteins. Visualization and modeling of these pADPr-associated proteins in networks not only reflect the widespread involvement of poly(ADP-ribosyl)ation in several pathways but also identify protein targets that could shed new light on the regulatory functions of pADPr in normal physiological conditions as well as after exposure to genotoxic stimuli.
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