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194 results on '"van Eynde, Aleyde"'

19. The Polycomb group protein EZH2 directly controls DNA methylation

Author

Viré, Emmanuelle, Brenner, Carmen, Deplus, Rachel, Blanchon, Loïc, Fraga, Mario, Didelot, Céline, Morey, Lluis, Van Eynde, Aleyde, Bernard, David, Vanderwinden, Jean-Marie, Bollen, Mathieu, Esteller, Manel, Di Croce, Luciano, de Launoit, Yvan, and Fuks, François

Published
2006

23. Overexpression of PP1-NIPP1 limits the capacity of cells to repair DNA double-strand breaks

Author

Winkler, Claudia, Rouget, Raphael, Wu, Dan, Beullens, Monique, Van Eynde, Aleyde, and Bollen, Mathieu

Subjects
enzymes and coenzymes (carbohydrates), fungi, NIPP1, DNA damage, DNA double-strand breaks, DNA repair, Replication stress, FHA domain, macromolecular substances, biological phenomena, cell phenomena, and immunity, Protein dephosphorylation, PP1
Abstract

The ubiquitously expressed nuclear protein NIPP1 (also known as PPP1R8) recruits phosphoproteins for regulated dephosphorylation by the associated protein phosphatase PP1. To bypass the PP1 titration artifacts seen upon NIPP1 overexpression, we have engineered covalently linked fusions of PP1 and NIPP1, and demonstrate their potential to selectively explore the function of the PP1:NIPP1 holoenzyme. By using inducible stable cell lines, we show that PP1-NIPP1 fusions cause replication stress in a manner that requires both PP1 activity and substrate recruitment via the ForkHead Associated domain of NIPP1. More specifically, PP1-NIPP1 expression resulted in the build up of RNA-DNA hybrids (R-loops), enhanced chromatin compaction and a diminished repair of DNA double-strand breaks (DSBs), culminating in the accumulation of DSBs. These effects were associated with a reduced expression of DNA damage signaling and repair proteins. Our data disclose a key role for dephosphorylation of PP1:NIPP1 substrates in setting the threshold for DNA repair, and indicate that activators of this phosphatase hold therapeutic potential as sensitizers for DNA-damaging agents. ispartof: JOURNAL OF CELL SCIENCE vol:131 issue:13 ispartof: location:England status: published

Published
2018

25. Correction: MELK-T1, a small-molecule inhibitor of protein kinase MELK, decreases DNA-damage tolerance in proliferating cancer cells

Author

Beke, Lijs, primary, Kig, Cenk, additional, Linders, Joannes T. M., additional, Boens, Shannah, additional, Boeckx, An, additional, van Heerde, Erika, additional, Parade, Marc, additional, De Bondt, An, additional, Van den Wyngaert, Ilse, additional, Bashir, Tarig, additional, Ogata, Souichi, additional, Meerpoel, Lieven, additional, Van Eynde, Aleyde, additional, Johnson, Christopher N., additional, Beullens, Monique, additional, Brehmer, Dirk, additional, and Bollen, Mathieu, additional

Published
2018
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27. The deletion of the phosphatase regulator NIPP1 causes progenitor cell expansion in the adult liver

Author

Boens, Shannah, Verbinnen, Iris, Verhulst, Stefaan, Szekér, Kathelijne, Ferreira, Monica, Gevaert, Thomas, Baes, Myriam, Roskams, Tania, van Grunsven, Leo A, Van Eynde, Aleyde, and Bollen, Mathieu

Abstract

The Ppp1r8 gene encodes NIPP1, a nuclear interactor of protein phosphatase PP1. The deletion of NIPP1 is embryonic lethal at the gastrulation stage, which has hampered its functional characterization in adult tissues. Here, we describe the effects of a conditional deletion of NIPP1 in mouse liver epithelial cells. Ppp1r8(-/-) livers developed a ductular reaction, i.e. bile-duct hyperplasia with associated fibrosis. The increased proliferation of biliary epithelial cells was at least partially due to an expansion of the progenitor cell compartment that was independent of liver injury. Gene-expression analysis confirmed an upregulation of progenitor cell markers in the liver knockout livers but showed no effect on the expression of liver-injury associated regulators of cholangiocyte differentiation markers. Consistent with an inhibitory effect of NIPP1 on progenitor cell proliferation, Ppp1r8(-/-) livers displayed an increased sensitivity to diet-supplemented 3,5-diethoxycarbonyl-1,4-dihydrocollidine, which also causes bile-duct hyperplasia through progenitor cell expansion. In contrast, the liver knockouts responded normally to injuries (partial hepatectomy, single CCl4 administration) that are restored through proliferation of differentiated parenchymal cells. Our data indicate that NIPP1 does not regulate the proliferation of hepatocytes but is a suppressor of biliary epithelial cell proliferation, including progenitor cells, in the adult liver. This article is protected by copyright. All rights reserved. ispartof: Stem Cells vol:34 issue:8 pages:2256-2262 ispartof: location:England status: published

Published
2016

29. The KH-Tudor domain of A-kinase anchoring protein 149 mediates RNA-dependent self-association

Author

Rogne, Marie, Landsverk, Helga B., Van Eynde, Aleyde, Beullens, Monique, Bollen, Mathieu, Collas, Philippe, and Kuntziger, Thomas

Subjects
RNA -- Atomic properties, RNA -- Physiological aspects, Cyclic adenosine monophosphate response element-binding protein -- Physiological aspects, Cyclic adenosine monophosphate response element-binding protein -- Chemical properties, Biological sciences, Chemistry
Abstract

The properties of the COOH-terminal domain of A-kinase anchoring protein 149 (AKAP149), which is found in mitochondria and in the endoplasmic reticulum-nuclear envelope network, are investigated. The results have shown that the KH-Tudor-containing domain of AKAP149 binds RNA in vitro and in RNA coprecipitation.

Published
2006

35. Advanced Microscopy Facility, Vienna Biocenter Core Facilities, Dr. Bohr-Gasse 3, 1030 Vienna, Austria.

Author

Winkler, Claudia, Rouget, Raphael, Wu, Dan, Beullens, Monique, Van Eynde, Aleyde, and Bollen, Mathieu

Subjects
NUCLEAR proteins, PHOSPHOPROTEINS, DEPHOSPHORYLATION, PHOSPHATASES, RNA, DNA, BIOCHEMICAL substrates
Abstract

The ubiquitously expressed nuclear protein NIPP1 (also known as PPP1R8) recruits phosphoproteins for regulated dephosphorylation by the associated protein phosphatase PP1. To bypass the PP1 titration artifacts seen upon NIPP1 overexpression, we have engineered covalently linked fusions of PP1 and NIPP1, and demonstrate their potential to selectively explore the function of the PP1:NIPP1 holoenzyme. By using inducible stable cell lines, we show that PP1--NIPP1 fusions cause replication stress in a manner that requires both PP1 activity and substrate recruitment via the ForkHead Associated domain of NIPP1. More specifically, PP1--NIPP1 expression resulted in the build up of RNA--DNA hybrids (R-loops), enhanced chromatin compaction and a diminished repair of DNA double-strand breaks (DSBs), culminating in the accumulation of DSBs. These effects were associated with a reduced expression of DNA damage signaling and repair proteins. Our data disclose a key role for dephosphorylation of PP1:NIPP1 substrates in setting the threshold for DNA repair, and indicate that activators of this phosphatase hold therapeutic potential as sensitizers for DNA-damaging agents. [ABSTRACT FROM AUTHOR]

Published
2018
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36. Molecular Cloning of NIPP-1, a Nuclear Inhibitor of Protein Phosphatase-1, Reveals Homology with Polypeptides Involved in RNA Processing

Author

Willy Stalmans, Stefaan Wera, Sophie Torrekens, Van Eynde Aleyde, Van Leuven Fred, Mathieu Bollen, and Monique Beullens

Subjects
DNA, Complementary, Protein subunit, Molecular Sequence Data, RNA-binding protein, Thymus Gland, Molecular cloning, Biology, Polymerase Chain Reaction, Biochemistry, Protein Phosphatase 1, Endoribonucleases, Phosphoprotein Phosphatases, Protein biosynthesis, Animals, Humans, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, RNA Processing, Post-Transcriptional, Protein kinase A, Molecular Biology, DNA Primers, Gene Library, Messenger RNA, Base Sequence, Sequence Homology, Amino Acid, Alternative splicing, Intracellular Signaling Peptides and Proteins, Proteins, RNA-Binding Proteins, Cell Biology, Molecular biology, Recombinant Proteins, Molecular Weight, Alternative Splicing, Liver, Oligodeoxyribonucleotides, Organ Specificity, Protein Biosynthesis, Cattle, Casein kinase 2, Carrier Proteins
Abstract

NIPP-1 was originally isolated as a potent and specific nuclear inhibitory polypeptide (16-18 kDa) of protein phosphatase-1. We report here the cDNA cloning of NIPP-1 from bovine thymus and show that the native polypeptide consists of 351 residues and has a calculated mass of 38.5 kDa. The bacterially expressed central third of NIPP-1 completely inhibited the type-1 catalytic subunit, but displayed a reduced inhibitory potency after phosphorylation by protein kinase A and casein kinase 2. Translation of NIPP-1 mRNA in reticulocyte lysates resulted in the accumulation of both intact NIPP-1 and a smaller polypeptide generated by alternative initiation at the codon corresponding to Met143. A data base search showed that the COOH terminus of NIPP-1 is nearly identical to the human ard-1 protein (13 kDa), which has been implicated in RNA processing (Wang, M., and Cohen, S. N. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 10591-10595). Comparison of the cDNAs encoding ard-1 and NIPP-1 suggests that their mRNAs are generated by alternative splicing of the same pre-mRNA. Western blotting with antibodies against the COOH terminus of NIPP-1, however, showed a single polypeptide of 47 kDa, which was enriched in the nucleus. Northern analysis revealed a single transcript of 2.2 kilobases in bovine thymus and of 2.4 kilobases in various human tissues.

Published
1995
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37. MELK-T1, a small-molecule inhibitor of protein kinase MELK, decreases DNA-damage tolerance in proliferating cancer cells

Author

Beke, Lijs, primary, Kig, Cenk, additional, Linders, Joannes T. M., additional, Boens, Shannah, additional, Boeckx, An, additional, van Heerde, Erika, additional, Parade, Marc, additional, De Bondt, An, additional, Van den Wyngaert, Ilse, additional, Bashir, Tarig, additional, Ogata, Souichi, additional, Meerpoel, Lieven, additional, Van Eynde, Aleyde, additional, Johnson, Christopher N., additional, Beullens, Monique, additional, Brehmer, Dirk, additional, and Bollen, Mathieu, additional

Published
2015
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38. DNA Methylation-Guided Prediction of Clinical Failure in High-Risk Prostate Cancer

Author

Litovkin, Kirill, primary, Van Eynde, Aleyde, additional, Joniau, Steven, additional, Lerut, Evelyne, additional, Laenen, Annouschka, additional, Gevaert, Thomas, additional, Gevaert, Olivier, additional, Spahn, Martin, additional, Kneitz, Burkhard, additional, Gramme, Pierre, additional, Helleputte, Thibault, additional, Isebaert, Sofie, additional, Haustermans, Karin, additional, and Bollen, Mathieu, additional

Published
2015
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42. Methylation-guided stratification of patients with high-risk prostate cancer for the prediction of clinical failure.

Author

Litovkin, Kirill, primary, Joniau, Steven, additional, Lerut, Evelyne, additional, Laenen, Annouschka, additional, Gevaert, Olivier, additional, Spahn, Martin, additional, Kneitz, Burkhard, additional, Isebaert, Sofie, additional, Haustermans, Karin, additional, Beullens, Monique, additional, Van Eynde, Aleyde, additional, and Bollen, Mathieu, additional

Published
2014
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44. The transcriptional repressor NIPP1 is an essential player in EZH2-mediated gene silencing.

Author

Nuytten, M, Beke, L, Van Eynde, Aleyde, Ceulemans, H, Beullens, M, Van Hummelen, Paul, Fuks, François, Bollen, M, Nuytten, M, Beke, L, Van Eynde, Aleyde, Ceulemans, H, Beullens, M, Van Hummelen, Paul, Fuks, François, and Bollen, M

Abstract

EZH2 is a Polycomb group (PcG) protein that promotes the late-stage development of cancer by silencing a specific set of genes, at least in part through trimethylation of associated histone H3 on Lys 27 (H3K27). Nuclear inhibitor of protein phosphatase-1 (NIPP1) is a ubiquitously expressed transcriptional repressor that has binding sites for the EZH2 interactor EED. Here, we examine the contribution of NIPP1 to EZH2-mediated gene silencing. Studies on NIPP1-deficient cells disclose a widespread and essential role of NIPP1 in the trimethylation of H3K27 by EZH2, not only in the onset of this trimethylation during embryonic development, but also in the maintenance of this repressive mark in proliferating cells. Consistent with this notion, EZH2 and NIPP1 silence a common set of genes, as revealed by gene-expression profiling, and NIPP1 is associated with established Polycomb target genes and with genomic regions that are enriched in Polycomb targets. Furthermore, most NIPP1 target genes are trimethylated on H3K27 and the knockdown of either NIPP1 or EZH2 is often associated with a loss of this modification. Our data reveal that NIPP1 is required for the global trimethylation of H3K27 and is implicated in gene silencing by EZH2., Comparative Study, Journal Article, Research Support, Non-U.S. Gov't, SCOPUS: ar.j, info:eu-repo/semantics/published

Published
2008

46. A Role for PP1/NIPP1 in Steering Migration of Human Cancer Cells

Author

Martin-Granados, Cristina, primary, Prescott, Alan R., additional, Van Dessel, Nele, additional, Van Eynde, Aleyde, additional, Arocena, Miguel, additional, Klaska, Izabela P., additional, Görnemann, Janina, additional, Beullens, Monique, additional, Bollen, Mathieu, additional, Forrester, John V., additional, and McCaig, Colin D., additional

Published
2012
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49. The Polycomb group protein EZH2 directly controls DNA methylation

Author

Vire, Emmanuelle, Brenner, Carmen, Deplus, Rachel, Blanchon, Loic, Fraga, Mario, Didelot, Celine, Morey, Lluis, Van Eynde, Aleyde, Bernard, David, Vanderwinden, Jean-Marie, Bollen, Mathieu, Esteller, Manel, Croce, Luciano Di, de Launoit, Yvan, and Fuks, Francois

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Emmanuelle Viré; Carmen Brenner; Rachel Deplus; Loïc Blanchon; Mario Fraga; Céline Didelot; Lluis Morey; Aleyde Van Eynde; David Bernard; Jean-Marie Vanderwinden; Mathieu Bollen; Manel Esteller; Luciano Di Croce; Yvan [...]

Published
2007
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50. Erratum: The Polycomb group protein EZH2 directly controls DNA methylation

Author

Viré, Emmanuelle, primary, Brenner, Carmen, additional, Deplus, Rachel, additional, Blanchon, Loïc, additional, Fraga, Mario, additional, Didelot, Céline, additional, Morey, Lluis, additional, Van Eynde, Aleyde, additional, Bernard, David, additional, Vanderwinden, Jean-Marie, additional, Bollen, Mathieu, additional, Esteller, Manel, additional, Croce, Luciano Di, additional, de Launoit, Yvan, additional, and Fuks, François, additional

Published
2007
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