Search

Your search keyword '"Vérène Stierlé"' showing total 6 results
Start Over Author "Vérène Stierlé" Topic biology
6 results on '"Vérène Stierlé"'

1. Divergent effects of translation termination factor eRF3A and nonsense-mediated mRNA decay factor UPF1 on the expression of uORF carrying mRNAs and ribosome protein genes

Author

Affaf Aliouat, Pauline François, Vérène Stierlé, Olivier Jean-Jean, Pierre Bertin, Samia Salhi, Isabelle Hatin, Olivier Namy, Adaptation Biologique et Vieillissement = Biological Adaptation and Ageing (B2A), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de génétique et microbiologie [Orsay] (IGM), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS), Département de Mathématiques et Applications - ENS Paris (DMA), Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris), Centre recherche en CardioVasculaire et Nutrition (C2VN), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Paris Seine (IBPS), Sorbonne Université (SU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), École normale supérieure - Paris (ENS Paris)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Génomique, Structure et Traduction (GST), Département Biologie des Génomes (DBG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), ANR-17-CE12-0024,Rescue_ribosome,Voies de sauvetage pour les ribosomes non recyclés(2017), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), and SERRE, Marie-Claude

Subjects
Ribosomal Proteins, eRF3, [SDV]Life Sciences [q-bio], Nonsense-mediated decay, MRNA Decay, nonsense-mediated mRNA decay, Biology, [SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Ribosome, Open Reading Frames, 03 medical and health sciences, 0302 clinical medicine, RNA, Messenger, Molecular Biology, Gene, Translation termination, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, ribosome protein genes, GSPT1, RNA, translation termination, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Cell Biology, Nonsense Mediated mRNA Decay, Cell biology, [SDV] Life Sciences [q-bio], Gene Expression Regulation, 030220 oncology & carcinogenesis, UPF1, Trans-Activators, RNA Helicases, Peptide Termination Factors, Research Paper, uORF
Abstract

International audience; In addition to its role in translation termination, eRF3A has been implicated in the nonsense-mediated mRNA decay (NMD) pathway through its interaction with UPF1. NMD is a RNA quality control mechanism, which detects and degrades aberrant mRNAs as well as some normal transcripts including those that harbour upstream open reading frames in their 5' leader sequence. In this study, we used RNA-sequencing and ribosome profiling to perform a genome wide analysis of the effect of either eRF3A or UPF1 depletion in human cells. Our bioinformatics analyses allow to delineate the features of the transcripts controlled by eRF3A and UPF1 and to compare the effect of each of these factors on gene expression. We find that eRF3A and UPF1 have very different impacts on the human transcriptome, less than 250 transcripts being targeted by both factors. We show that eRF3A depletion globally derepresses the expression of mRNAs containing translated uORFs while UPF1 knockdown derepresses only the mRNAs harbouring uORFs with an AUG codon in an optimal context for translation initiation. Finally, we also find that eRF3A and UPF1 have opposite effects on ribosome protein gene expression. Together, our results provide important elements for understanding the impact of translation termination and NMD on the human transcriptome and reveal novel determinants of ribosome biogenesis regulation.

Published
2019
Full Text
View/download PDF

2. Perturbation of membrane microdomains in GLC4 multidrug-resistant lung cancer cells − modification of ABCC1 (MRP1) localization and functionality

Author

Carole Marbeuf-Gueye, Paiwan Sudwan, Arlette Garnier-Suillerot, Vérène Stierlé, and Milena Salerno

Subjects
0303 health sciences, biology, Cholesterol, Peripheral membrane protein, Cell Biology, Biochemistry, 3. Good health, Cell biology, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, Membrane, chemistry, 030220 oncology & carcinogenesis, ABCC1, biology.protein, Membrane fluidity, Lipid bilayer, Molecular Biology, Integral membrane protein, Lipid raft, 030304 developmental biology
Abstract

The multidrug resistance-associated protein transporter ABCC1 (MRP1) is an integral plasma membrane protein involved in the multidrug resistance phenotype. It actively expels a number of cytotoxic molecules from cells. To gain insight into the modulation of the functional properties of this integral membrane protein by cholesterol, a main component of the lipid bilayer, we used multidrug-resistant GLC4/ADR cells, which overexpress MRP1. Upon altering the plasma membrane cholesterol content of these cells, membrane localization and the activity of MRP1 were analyzed. A detergent-free methodology was used to separate ‘light’ and ‘heavy’ plasma membrane fractions. Our data show that MRP1 was exclusively found in ‘light’ fractions known as L0 phase membrane microdomains, together with ∼ 23% of gangliosides GM1 and 40% of caveolin-1. Depletion of the membrane cholesterol level to 40% by treatment with the cholesterol-chelating agent methyl-β-cyclodextrin did not modify MRP1 activity, as evidenced either by the rate of efflux of pirarubicin or that of glutathione. Further cholesterol depletion below 40% yielded both a partial shift of MRP1 to the high-density fraction and a decrease of its functionality. Taken together, these data suggest that MRP1 funtionality depends on its localization in cholesterol-rich membrane microdomains.

Published
2007
Full Text
View/download PDF

3. Modulation of MDR1 gene expression in multidrug resistant MCF7 cells by low concentrations of small interfering RNAs

Author

Vérène Stierlé, Alain Laigle, and Béatrice Jolles

Subjects
Small interfering RNA, ATP Binding Cassette Transporter, Subfamily B, Time Factors, Cell Survival, Cell, Down-Regulation, Gene Expression, Cell Count, Biology, Biochemistry, Fluorescence, RNA interference, Cell Line, Tumor, Gene expression, medicine, Humans, Gene silencing, Doxorubicin, RNA, Messenger, RNA, Small Interfering, P-glycoprotein, Pharmacology, Cell Death, Dose-Response Relationship, Drug, Daunorubicin, Trypan Blue, Flow Cytometry, Molecular biology, Multiple drug resistance, medicine.anatomical_structure, Verapamil, biology.protein, Genes, MDR, medicine.drug
Abstract

MDR1 overexpression is one form of the multidrug resistance (MDR) phenotype, which can be acquired by patients initially responsive to chemotherapy. Because of the high toxicity of the inhibitors of P-glycoprotein (P-gp), the protein encoded by MDR1, attention has been focused on selective modulation of the MDR1 gene. Small interfering RNAs (siRNAs) were shown to be powerful tools for such a purpose, even when used at low concentrations (< or =20 nM) in order to avoid sequence nonspecific effects. Two siRNAs used at 20 nM were shown to lead to efficient down-regulation of MDR1 at the protein level (only ca. 20% total P-gp expression remaining) in the doxorubicin selected MCF7-R human cell line. Cell surface expression of P-gp was inhibited, leading to reversal of the drug efflux phenotype (about 40% reversal with the most efficient siRNA) and enhancement of chemosensitivity (about 35%). At the mRNA level, the down-regulation of MDR1 obtained with the most efficient siRNA increased from about 50% (5 nM siRNA) to 60% (10 or 20 nM). The advantage of using a combination of siRNAs instead of a single one has been suggested.

Published
2005
Full Text
View/download PDF

4. The Reduction of P-Glycoprotein Expression by Small Interfering RNAs Is Improved in Exponentially Growing Cells

Author

Vérène Stierlé, Alain Laigle, and Béatrice Jollès

Subjects
Small interfering RNA, Cell growth, Trans-acting siRNA, Gene Expression, RNA, Transfection, Biology, Drug Resistance, Multiple, Cell biology, Mice, RNA interference, Cell culture, Tumor Cells, Cultured, Genetics, Animals, Humans, Molecular Medicine, Gene silencing, RNA Interference, ATP Binding Cassette Transporter, Subfamily B, Member 1, Genes, MDR, RNA, Small Interfering, Molecular Biology
Abstract

Small interfering RNAs (siRNAs) are powerful tools in specifically silencing gene expression. Nevertheless, their efficiency can be limited when targeting proteins with an unusually long half-life, such as P-glycoprotein (P-gp), which is involved in the multidrug resistance phenomenon. P-gp is characterized by a long half-life, which may vary depending on the cell line and, for some of them, on serum deprivation or high cell density. In the present paper, involvement of an exponential cell growth phase in the improvement of siRNA efficiency has been suggested. The doxorubicin-selected human line MCF7-R was shown to be a more adapted model than NIH-MDR-G185 cells stably transfected with human mdr1. Nonspecific effects occurring at moderate (100 nM) siRNA concentration have been shown. Two efficient siRNAs led to a very satisfactory P-gp extinction (only 20% P-gp expression remaining) with siRNA concentration as low as 20 nM.

Published
2004
Full Text
View/download PDF

5. Auxin-Binding Protein 1 is a negative regulator of the SCF(TIR1/AFB) pathway

Author

Pascal Genschik, Vérène Stierlé, Philippe Muller, Anne-Laure Quettier, Alexandre Tromas, Catherine Perrot-Rechenmann, Esther Lechner, Sébastien Paque, Institut des sciences du végétal (ISV), Centre National de la Recherche Scientifique (CNRS), Matrice extracellulaire et dynamique cellulaire - UMR 7369 (MEDyC), Université de Reims Champagne-Ardenne (URCA)-SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Centre National de la Recherche Scientifique (CNRS), Centre Interdisciplinaire de Nanoscience de Marseille (CINaM), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie moléculaire des plantes (IBMP), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), ANR-08-BLAN-0219,AMUCCAS,ABP1 Modulation of Ubiquitin mediated protein degradation in Cell Cycle and Auxin Signalling(2008), SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Centre National de la Recherche Scientifique (CNRS), Université de Reims Champagne-Ardenne (URCA)-Université de Reims Champagne-Ardenne (URCA)-Centre National de la Recherche Scientifique (CNRS), and Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
0106 biological sciences, Transcription, Genetic, Arabidopsis, General Physics and Astronomy, Repressor, Receptors, Cell Surface, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Endocytosis, 01 natural sciences, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, Gene Expression Regulation, Plant, Auxin, heterocyclic compounds, Receptor, Plant Proteins, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Gene knockdown, Multidisciplinary, Indoleacetic Acids, biology, Arabidopsis Proteins, Protein Stability, F-Box Proteins, fungi, Gene Expression Regulation, Developmental, food and beverages, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, General Chemistry, biology.organism_classification, Transport inhibitor, Ubiquitin ligase, chemistry, Biochemistry, Plant signalling, Proteolysis, biology.protein, Plant hormone, Signal Transduction, 010606 plant biology & botany
Abstract

International audience; Auxin is a major plant hormone that controls most aspects of plant growth and development. Auxin is perceived by two distinct classes of receptors: transport inhibitor response 1 (TIR1, or auxin-related F-box (AFB)) and auxin/indole-3-acetic acid (AUX/IAA) coreceptors, that control transcriptional responses to auxin, and the auxin-binding protein 1 (ABP1), that controls a wide variety of growth and developmental processes. To date, the mode of action of ABP1 is still poorly understood and its functional interaction with TIR1/AFB-AUX/IAA coreceptors remains elusive. Here we combine genetic and biochemical approaches to gain insight into the integration of these two pathways. We find that ABP1 is genetically upstream of TIR1/AFBs; ABP1 knockdown leads to an enhanced degradation of AUX/IAA repressors, independently of its effects on endocytosis, through the SCF TIR1/AFB E3 ubiquitin ligase pathway. Combining positive and negative regulation of SCF ubiquitin-dependent pathways might be a common mechanism conferring tight control of hormone-mediated responses.

Published
2013
Full Text
View/download PDF

6. Targeting MDR1 gene: synthesis and cellular study of modified daunomycin-triplex-forming oligonucleotide conjugates able to inhibit gene expression in resistant cell lines

Author

Vérène Stierlé, Maria Duca, Ludovic Halby, Catherine Senamaud-Beaufort, Massimo L. Capobianco, Paola B. Arimondo, Béatrice Jollès, Alain Laigle, Matrice extracellulaire et dynamique cellulaire - UMR 7369 (MEDyC), Université de Reims Champagne-Ardenne (URCA)-SFR CAP Santé (Champagne-Ardenne Picardie Santé), and Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Molecular Sequence Data, Oligonucleotides, Down-Regulation, Electrophoretic Mobility Shift Assay, Drug resistance, Biology, Transfection, ANTISENSE OLIGONUCLEOTIDES, 03 medical and health sciences, Exon, Mice, 0302 clinical medicine, Western blot, Cell Line, Tumor, Gene expression, medicine, Moiety, Animals, Humans, ATP Binding Cassette Transporter, Subfamily B, Member 1, DAUNOMYCIN-TFO, CANCER-CELLS, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Pharmacology, 0303 health sciences, medicine.diagnostic_test, Base Sequence, Oligonucleotide, Daunorubicin, C-MYC GENE, DNA, MULTIPLE-DRUG RESISTANCE, Phenotype, Molecular biology, 3. Good health, Gene Expression Regulation, Neoplastic, Kinetics, Spectrometry, Fluorescence, Drug Resistance, Neoplasm, 030220 oncology & carcinogenesis, NIH 3T3 Cells, Molecular Medicine, Conjugate
Abstract

Reversal of the multidrug-resistant (MDR) phenotype is very important for chemotherapy success. In fact, the expression of the MDR1 gene-encoded P-glycoprotein (P-gp) actively expels antitumor agents such as daunomycin (DNM) out of the cells, resulting in drug resistance. We show that upon conjugation to triplex-forming oligonucleotides, it is possible to address DNM in resistant cells (MCF7-R and NIH-MDR-G185). The oligonucleotide moiety of the conjugate changes the cellular penetration properties of the antitumor agent that is no more the target of P-gp in resistant cells. We observe an accumulation of conjugated DNM in cells up to 72 h. For more efficient delivery in the cells' nuclei, transfectant agents must be used. In addition, the conjugate recognizes a sequence located in exon 3 of MDR1 , and it inhibits its gene expression as measured both by Western blot and by reverse transcription-polymerase chain reaction.

Published
2008
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results