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

被引:0
作者
Pic, Emilie [1 ]
Gagne, Jean-Philippe [1 ]
Poirier, Guy G. [1 ]
机构
[1] Univ Laval, Fac Med, CHUQ Pavillon CHUL, Ctr Rech, Quebec City, PQ G1V 4G2, Canada
关键词
mass spectrometry; poly(ADP-ribose); poly(ADP-ribose) polymerase-1; post-translational modification; proteomics; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEINS; WERNER-SYNDROME PROTEIN; DNA-REPAIR; RIBOSE POLYMERASE; GENE-EXPRESSION; TRANSCRIPTIONAL REGULATION; PHOSPHOPROTEOMIC ANALYSIS; LYSINE ACETYLATION; SUMO MODIFICATIONS; OXIDATIVE STRESS;
D O I
10.1586/EPR.11.63
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
PARP-1 is an abundant nuclear protein that plays an essential role in the regulation of many genome integrity and chromatin-based processes, such as DNA repair, replication or transcriptional regulation. PARP-1 modulates the function of chromatin and nuclear proteins through several poly(ADP-ribose) (pADPr)-dependent pathways. Aside from the clearly established role of PARP-1 in the maintenance of genome stability, PARP-1 also emerged as an important regulator that links chromatin functions with extranuclear compartments. pADPr signaling has notably been found to be responsible for PARP-1-mediated mitochondrial dysfunction and cell death. Defining the mechanisms that govern the intrinsic functions of PARP-1 is fundamental to the understanding of signaling networks regulated by pADPr. The emergence of mass spectrometry-based proteomics and its broad applications in the study of biological systems represents an outstanding opportunity to widen our knowledge of the functional spectrum of PARP-1. In this article, we summarize various PARP-1 targeted proteomics studies and proteome-wide analyses that shed light on its protein interaction partners, expression levels and post-translational modifications.
引用
收藏
页码:759 / 774
页数:16
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