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PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation

Item Type:Article
Title:PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation
Creators Name:Yu, M. and Schreek, S. and Cerni, C. and Schamberger, C. and Lesniewicz, K. and Poreba, E. and Vervoorts, J. and Walsemann, G. and Groetzinger, J. and Kremmer, E. and Mehraein, Y. and Mertsching, J. and Kraft, R. and Austen, M. and Luscher-Firzlaff, J. and Luescher, B.
Abstract:The proto-oncoprotein c-Myc functions as a transcriptional regulator that controls different aspects of cell behavior, including proliferation, differentiation, and apoptosis. In addition, Myc proteins have the potential to transform cells and are deregulated in the majority of human cancers. Several Myc-interacting factors have been described that mediate part of Myc's functions in the control of cell behavior. Here, we describe the isolation of a novel 150kDa protein, designated PARP-10, that interacts with Myc. PAMP-10 possesses domains with homology to RNA recognition motifs and to poly(ADP-ribose) polymerases (PARP). Molecular modeling and biochemical analysis define a PARP domain that is capable of ADP-ribosylating PARP-10 itself and core histones, but neither Myc nor Max. PARP-10 is localized to the nuclear and cytoplasmic compartments that is controlled at least in part by a Leu-rich nuclear export sequence (NES). Functionally, PARP-10 inhibits c-Myc- and E1A-mediated cotransformation of rat embryo fibroblasts, a function that is independent of PARP activity but that depends on a functional NES. Together, our findings define a novel PARP enzyme involved in the control of cell proliferation.
Keywords:Myc, PARP, Transcription, Transformation
Publisher:Nature Publishing Group
Page Range:1982-1993
Date:1 January 2005
Official Publication:https://doi.org/10.1038/sj.onc.1208410
PubMed:View item in PubMed

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