Mass spectrometry-based functional proteomics of poly(ADP-ribose) polymerase-1. (December 2011)

• Record Type: Journal Article
• Authors: Pic, Emilie; Gagné, Jean-Philippe; Poirier, Guy G
• Is Part Of: Expert review of proteomics. Volume 8:Number 6(2011)
• Page Start: 759
• Page End: 774
• Publication Date: 2011-12
• Subjects: mass spectrometry -- poly(ADP-ribose) -- poly(ADP-ribose) polymerase-1 -- post-translational modification -- proteomics; Proteins -- Biotechnology -- Periodicals; Proteomics -- Periodicals; 572.6
• DOI: 10.1586/epr.11.63
• Languages: English
• ISSNs: 1478-9450

Abstract

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.