Mass spectrometry-based functional proteomics of poly(ADP-ribose) polymerase-1.

作者: Emilie Pic , Jean-Philippe Gagné , Guy G Poirier , None

DOI: 10.1586/EPR.11.63

关键词:

摘要: PARP-1 is an abundant nuclear protein that plays essential role in the regulation of many genome integrity and chromatin-based processes, such as DNA repair, replication or transcriptional regulation. modulates function chromatin proteins through several poly(ADP-ribose) (pADPr)-dependent pathways. Aside from clearly established maintenance stability, also emerged important regulator links functions with extranuclear compartments. pADPr signaling has notably been found to be responsible for PARP-1-mediated mitochondrial dysfunction cell death. Defining mechanisms govern intrinsic fundamental understanding networks regulated by pADPr. The emergence mass spectrometry-based proteomics its broad applications study biological systems represents outstanding opportunity widen our knowledge functional spectrum PARP-1. In this arti...

参考文章(168)
Yunmin Li, Hyun Ju Oh, Yun-Fai Chris Lau, The poly(ADP-ribose) polymerase 1 interacts with Sry and modulates its biological functions Molecular and Cellular Endocrinology. ,vol. 257-258, pp. 35- 46 ,(2006) , 10.1016/J.MCE.2006.06.008
Nadine Martin, Klaus Schwamborn, Valérie Schreiber, Andreas Werner, Christelle Guillier, Xiang-Dong Zhang, Oliver Bischof, Jacob-S Seeler, Anne Dejean, PARP-1 transcriptional activity is regulated by sumoylation upon heat shock The EMBO Journal. ,vol. 28, pp. 3534- 3548 ,(2009) , 10.1038/EMBOJ.2009.279
Hyunju Ryu, Gada Al-Ani, Katelyn Deckert, Donald Kirkpatrick, Steven P. Gygi, Mary Dasso, Yoshiaki Azuma, PIASy Mediates SUMO-2/3 Conjugation of Poly(ADP-ribose) Polymerase 1 (PARP1) on Mitotic Chromosomes Journal of Biological Chemistry. ,vol. 285, pp. 14415- 14423 ,(2010) , 10.1074/JBC.M109.074583
Zhihua Tao, Peng Gao, Hung-wen Liu, Identification of the ADP-ribosylation sites in the PARP-1 automodification domain: analysis and implications. Journal of the American Chemical Society. ,vol. 131, pp. 14258- 14260 ,(2009) , 10.1021/JA906135D
Philipp Mayer-Kuckuk, Oliver Ullrich, Mathias Ziegler, Tilman Grune, Manfred Schweiger, Functional interaction of poly(ADP-ribose) with the 20S proteasome in vitro. Biochemical and Biophysical Research Communications. ,vol. 259, pp. 576- 581 ,(1999) , 10.1006/BBRC.1999.0824
Jean-Philippe Gagné, Xavier Moreel, Pierre Gagné, Yves Labelle, Arnaud Droit, Mélissa Chevalier-Paré, Sylvie Bourassa, Darin McDonald, Michael J. Hendzel, Claude Prigent, Guy G. Poirier, Proteomic investigation of phosphorylation sites in poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase. Journal of Proteome Research. ,vol. 8, pp. 1014- 1029 ,(2009) , 10.1021/PR800810N
C. Choudhary, C. Kumar, F. Gnad, M. L. Nielsen, M. Rehman, T. C. Walther, J. V. Olsen, M. Mann, Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions Science. ,vol. 325, pp. 834- 840 ,(2009) , 10.1126/SCIENCE.1175371
T. M. Kauppinen, W. Y. Chan, S. W. Suh, A. K. Wiggins, E. J. Huang, R. A. Swanson, Direct phosphorylation and regulation of poly(ADP-ribose) polymerase-1 by extracellular signal-regulated kinases 1/2 Proceedings of the National Academy of Sciences of the United States of America. ,vol. 103, pp. 7136- 7141 ,(2006) , 10.1073/PNAS.0508606103
Sanjay Navani, The human protein atlas The Journal of Obstetrics and Gynecology of India. ,vol. 61, pp. 27- 31 ,(2011) , 10.1007/S13224-011-0013-Z
Henri A. Blomster, Ville Hietakangas, Jianmin Wu, Petri Kouvonen, Sampsa Hautaniemi, Lea Sistonen, Novel proteomics strategy brings insight into the prevalence of SUMO-2 target sites Molecular & Cellular Proteomics. ,vol. 8, pp. 1382- 1390 ,(2009) , 10.1074/MCP.M800551-MCP200