At the Interface of Three Nucleic Acids: The Role of RNA-Binding Proteins and Poly(ADP-ribose) in DNA Repair

Alemasova, Elizaveta E.; Lavrik, Olga I.

doi:10.32607/20758251-2017-9-2-4-16

Cited by 13 publications

(11 citation statements)

References 194 publications

(226 reference statements)

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“…39,43 A role for FOXL2 in these crucial processes is supported by its interaction with HNRNPUL2 (Heterogeneous Nuclear Ribonucleoprotein U-like Protein 2), which promotes DNA double strand break signaling and repair 44 and with the helicase XRCC6 (KU70) involved in double strand DNA repair 45,46 and probably in telomeric stability. [50][51][52] ESR1 is a known FOXL2 co-factor, 20 and our MS data identify other major actors of this process: TOP2B, XRCC6, RNA Pol II (eight subunits of the RNA polymerase II holoenzyme complex), F I G U R E 6 Analysis of alternative splicing events (ASEs) upon FOXL2 knockdown. We have previously shown that the interaction of XRCC6 with FOXL2 leads to an inhibition of the transactivation ability of the latter on several reporter promoters and its apoptosis-inducing capacity, suggesting a potential implication in granulosa cell tumorigenesis.…”

Section: Discussionmentioning

confidence: 83%

Conventional and unconventional interactions of the transcription factor FOXL2 uncovered by a proteome‐wide analysis

et al. 2019

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Beyond the study of its transcriptional target genes, the identification of the various interactors of a transcription factor (TF) is crucial to understand its diverse cellular roles. We focused on FOXL2, a winged‐helix forkhead TF important for ovarian development and maintenance. FOXL2 has been implicated in diverse cellular processes, including apoptosis, the control of cell cycle or the regulation of steroid hormone synthesis. To reliably identify partners of endogenous FOXL2, we performed a proteome‐wide analysis using co‐immunoprecipitation in the murine granulosa cell‐derived AT29c and the pituitary‐derived alpha‐T3 cell lines, using three antibodies targeting different parts of the protein. Following a stringent selection of mass spectrometry data on the basis of identification reliability and protein enrichment, we identified a core set of 255 partners common to both cell lines. Their analysis showed that we could co‐precipitate several complexes involved in mRNA processing, chromatin remodeling and DNA replication and repair. We further validated (direct and/or indirect) interactions with selected partners, suggesting an unexpected role for FOXL2 in those processes. Overall, this comprehensive analysis of the endogenous FOXL2 interactome sheds light on its numerous and diverse interactors and unconventional cellular roles.

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Section: Discussionmentioning

confidence: 83%

Conventional and unconventional interactions of the transcription factor FOXL2 uncovered by a proteome‐wide analysis

et al. 2019

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“…All these events have to be regulated by protein-DNA and protein-protein interactions as well as by interactions of proteins with poly(ADP-ribose). It is known that the function of RNA-binding proteins is also dependent on PARP and poly(ADP-ribosyl)ation (27,114).…”

Section: Discussionmentioning

confidence: 99%

Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins

Alemasova

Lavrik

2019

Nucleic Acids Research

353

243

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Poly(ADP-ribosyl)ation (PARylation) is posttranslational modification of proteins by linear or branched chains of ADP-ribose units, originating from NAD+. The central enzyme for PAR production in cells and the main target of poly(ADP-ribosyl)ation during DNA damage is poly(ADP-ribose) polymerase 1 (PARP1). PARP1 ability to function as a catalytic and acceptor protein simultaneously made a considerable contribution to accumulation of contradictory data. This topic is directly related to other questions, such as the stoichiometry of PARP1 molecules in auto-modification reaction, direction of the chain growth during PAR elongation and functional coupling of PARP1 with PARylation targets. Besides DNA damage necessary for the folding of catalytically active PARP1, other mechanisms appear to be required for the relevant intensity and specificity of PARylation reaction. Indeed, in recent years, PARP research has been enriched by the discovery of novel PARP1 interaction partners modulating its enzymatic activity. Understanding the details of PARP1 catalytic mechanism and its regulation is especially important in light of PARP-targeted therapy and may significantly aid to PARP inhibitors drug design. In this review we summarize old and up-to-date literature to clarify several points concerning PARylation mechanism and discuss different ways for regulation of PAR synthesis by accessory proteins reported thus far.

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“…PARP1 could be activated by phosphorylation (594), by direct protein/protein interaction (595), and by ADP-ribosylation by PARP3 (45). An interaction with YB-1 was shown to control the level of PARylation depending on the significance of DNA damage (596). The full biological significance and molecular mechanisms of these alternate roles remain to be elucidated.…”

Section: Coupling Dna Damage Detection To Catalytic Activitymentioning

confidence: 99%

Poly(ADP-Ribose) Polymerases in Host-Pathogen Interactions, Inflammation, and Immunity

Brady

Goel

Johnson

2019

Microbiol Mol Biol Rev

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SUMMARYThe literature review presented here details recent research involving members of the poly(ADP-ribose) polymerase (PARP) family of proteins. Among the 17 recognized members of the family, the human enzyme PARP1 is the most extensively studied, resulting in a number of known biological and metabolic roles. This review is focused on the roles played by PARP enzymes in host-pathogen interactions and in diseases with an associated inflammatory response. In mammalian cells, several PARPs have specific roles in the antiviral response; this is perhaps best illustrated by PARP13, also termed the zinc finger antiviral protein (ZAP). Plant stress responses and immunity are also regulated by poly(ADP-ribosyl)ation. PARPs promote inflammatory responses by stimulating proinflammatory signal transduction pathways that lead to the expression of cytokines and cell adhesion molecules. Hence, PARP inhibitors show promise in the treatment of inflammatory disorders and conditions with an inflammatory component, such as diabetes, arthritis, and stroke. These functions are correlated with the biophysical characteristics of PARP family enzymes. This work is important in providing a comprehensive understanding of the molecular basis of pathogenesis and host responses, as well as in the identification of inhibitors. This is important because the identification of inhibitors has been shown to be effective in arresting the progression of disease.

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At the Interface of Three Nucleic Acids: The Role of RNA-Binding Proteins and Poly(ADP-ribose) in DNA Repair

Cited by 13 publications

References 194 publications

Conventional and unconventional interactions of the transcription factor FOXL2 uncovered by a proteome‐wide analysis

Conventional and unconventional interactions of the transcription factor FOXL2 uncovered by a proteome‐wide analysis

Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins

Poly(ADP-Ribose) Polymerases in Host-Pathogen Interactions, Inflammation, and Immunity

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