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Your search keyword '"MESH : RNA Splicing"' showing total 6 results
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6 results on '"MESH : RNA Splicing"'

1. Functional characterization of the AFF (AF4/FMR2) family of RNA-binding proteins: insights into the molecular pathology of FRAXE intellectual disability

Author

Mireille Melko, Samantha Zongaro, Jozef Gecz, Dominique Douguet, Barbara Bardoni, Céline Verheggen, Mounia Bensaid, Institut de pharmacologie moléculaire et cellulaire ( IPMC ), Université Nice Sophia Antipolis ( UNS ), Université Côte d'Azur ( UCA ) -Université Côte d'Azur ( UCA ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de Génétique Moléculaire de Montpellier ( IGMM ), Centre National de la Recherche Scientifique ( CNRS ) -Université de Montpellier ( UM ), Department of Genetic Medicine Women's and Children's, University of Adelaide, Université Côte d'Azur ( UCA ), Institut de pharmacologie moléculaire et cellulaire (IPMC), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), and COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)

Subjects
MESH : Cell Line, MESH : Molecular Sequence Data, MESH: Sequence Homology, Amino Acid, Gene Expression, RNA-binding protein, MESH: Amino Acid Sequence, MESH: Gene Order, Exon, 0302 clinical medicine, MESH : Protein Transport, Genes, Reporter, Transcription (biology), Gene Order, Genetics (clinical), Genetics, 0303 health sciences, MESH : Amino Acid Sequence, MESH : Sequence Alignment, RNA-Binding Proteins, General Medicine, MESH : Genes, Reporter, Phenotype, MESH : Sequence Homology, Amino Acid, DNA-Binding Proteins, Protein Transport, MESH : Fragile X Syndrome, 030220 oncology & carcinogenesis, RNA splicing, MESH : RNA Splicing, MESH : DNA-Binding Proteins, Intranuclear Space, MESH: Fragile X Syndrome, MESH: Protein Transport, MESH: Gene Expression, RNA Splicing, Molecular Sequence Data, MESH : RNA-Binding Proteins, MESH: Sequence Alignment, MESH: Intranuclear Space, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Cell Line, 03 medical and health sciences, MESH : Fibroblasts, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH : HeLa Cells, Amino Acid Sequence, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, Gene, 030304 developmental biology, MESH: Molecular Sequence Data, MESH: Humans, MESH : Gene Order, Sequence Homology, Amino Acid, [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology, MESH: Genes, Reporter, MESH : Humans, Alternative splicing, RNA, Fibroblasts, MESH: Cell Line, MESH : Gene Expression, MESH: RNA-Binding Proteins, MESH : Intranuclear Space, MESH: Fibroblasts, Fragile X Syndrome, MESH: HeLa Cells, MESH: RNA Splicing, Sequence Alignment, MESH: DNA-Binding Proteins, HeLa Cells
Abstract

International audience; The AFF (AF4/FMR2) family of genes includes four members: AFF1/AF4, AFF2/FMR2, AFF3/LAF4 and AFF4/AF5q31. AFF2/FMR2 is silenced in FRAXE intellectual disability, while the other three members have been reported to form fusion genes as a consequence of chromosome translocations with the myeloid/lymphoid or mixed lineage leukemia (MLL) gene in acute lymphoblastic leukemias (ALLs). All AFF proteins are localized in the nucleus and their role as transcriptional activators with a positive action on RNA elongation was primarily studied. We have recently shown that AFF2/FMR2 localizes to nuclear speckles, subnuclear structures considered as storage/modification sites of pre-mRNA splicing factors, and modulates alternative splicing via the interaction with the G-quadruplex RNA-forming structure. We show here that similarly to AFF2/FMR2, AFF3/LAF4 and AFF4/AF5q31 localize to nuclear speckles and are able to bind RNA, having a high apparent affinity for the G-quadruplex structure. Interestingly, AFF3/LAF4 and AFF4/AF5q31, like AFF2/FMR2, modulate, in vivo, the splicing efficiency of a mini-gene containing a G-quadruplex structure in one alternatively spliced exon. Furthermore, we observed that the overexpression of AFF2/3/4 interferes with the organization and/or biogenesis of nuclear speckles. These findings fit well with our observation that enlarged nuclear speckles are present in FRAXE fibroblasts. Furthermore, our findings suggest functional redundancy among the AFF family members in the regulation of splicing and transcription. It is possible that other members of the AFF family compensate for the loss of AFF2/FMR2 activity and as such explain the relatively mild to borderline phenotype observed in FRAXE patients.

Published
2011
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2. A key role for stress-induced satellite III transcripts in the relocalization of splicing factors into nuclear stress granules

Author

Jamal Tazi, Alexandra Metz, Johann Soret, Caroline Jolly, Claire Vourc'h, Institut d'oncologie/développement Albert Bonniot de Grenoble (INSERM U823), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Génétique Moléculaire de Montpellier (IGMM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), INSERM U823, équipe 10 (Stress et Dynamique de l'Organisation du Génome), Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Joseph Fourier - Grenoble 1 (UJF)-CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Souchier, Catherine, Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Institut d'oncologie/développement Albert Bonniot de Grenoble ( INSERM U823 ), Université Joseph Fourier - Grenoble 1 ( UJF ) -CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Institut de Génétique Moléculaire de Montpellier ( IGMM ), Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), Université Joseph Fourier - Grenoble 1 ( UJF ) -CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université Joseph Fourier - Grenoble 1 ( UJF ) -CHU Grenoble-EFS-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Institut National de la Santé et de la Recherche Médicale (INSERM)-EFS-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF), and Institut National de la Santé et de la Recherche Médicale (INSERM)-EFS-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM)-EFS-CHU Grenoble-Université Joseph Fourier - Grenoble 1 (UJF)

Subjects
MESH : Transcription Factors, MESH : Hela Cells, MESH: 3T3 Cells, MESH: Tubulin, MESH : Cell Cycle Proteins, 0302 clinical medicine, Heat Shock Transcription Factors, MESH : Leupeptins, Transcription (biology), MESH : Cell Nucleus Structures, MESH: Animals, Satellite III transcripts, HSF1, MESH: HSP70 Heat-Shock Proteins, MESH : Ubiquitin, 0303 health sciences, MESH : Ribonucleoproteins, Small Nuclear, Serine-Arginine Splicing Factors, MESH : Histone Deacetylases, Nuclear Proteins, RNA-Binding Proteins, MESH : Protein Binding, MESH: Transcription Factors, MESH : Tubulin, MESH : HSP90 Heat-Shock Proteins, Ribonucleoproteins, Small Nuclear, MESH : Heat-Shock Response, MESH: DNA, Satellite, DNA-Binding Proteins, Heat shock, RNA splicing, RNA Polymerase II, MESH : RNA Polymerase II, MESH : RNA Splicing, MESH : DNA-Binding Proteins, MESH: Molecular Chaperones, MESH: Acetylation, MESH : 3T3 Cells, MESH : Protein Folding, MESH: Ubiquitin, RNA Splicing, MESH: Protein Folding, MESH : RNA-Binding Proteins, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, DNA, Satellite, Biology, MESH : Acetylation, MESH: Phosphoproteins, 03 medical and health sciences, MESH: Cell Cycle Proteins, SR protein, Stress granule, Heat shock protein, MESH : Mice, MESH: Adenosine Triphosphatases, MESH: HSP90 Heat-Shock Proteins, Humans, MESH: Protein Binding, HSP70 Heat-Shock Proteins, Nuclear stress granules, snRNP, MESH: Cell Nucleus Structures, MESH: Mice, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, 030304 developmental biology, MESH : DNA, Satellite, MESH: Humans, MESH : Adenosine Triphosphatases, [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology, MESH: Ribonucleoproteins, Small Nuclear, MESH : Humans, MESH : Molecular Chaperones, MESH : Nuclear Proteins, MESH : HSP70 Heat-Shock Proteins, MESH: Leupeptins, Cell Biology, Phosphoproteins, Molecular biology, Cell Nucleus Structures, MESH: RNA Polymerase II, MESH: Hela Cells, MESH: Histone Deacetylases, Heat shock factor, MESH: RNA-Binding Proteins, MESH: Heat-Shock Response, MESH : Animals, MESH : Phosphoproteins, MESH: RNA Splicing, MESH: Nuclear Proteins, SR proteins, MESH: DNA-Binding Proteins, 030217 neurology & neurosurgery, HeLa Cells, Transcription Factors
Abstract

International audience; Exposure of cells to stressful conditions results in the rapid synthesis of a subset of specialized proteins termed heat shock proteins (HSPs) which function in protecting the cell against damage. The stress-induced activation of hsp genes is controlled by the heat shock transcription factor 1 (HSF1). At the cellular level, one of the most striking effects of stress is the rapid and reversible redistribution of HSF1 into a few nuclear structures termed nuclear stress granules which form primarily on the 9q12 locus in humans. Within these structures, HSF1 binds to satellite III repeated elements and drives the RNA polymerase II-dependent transcription of these sequences into stable RNAs which remain associated with the 9q12 locus for a certain time after synthesis. Other proteins, in particular splicing factors, were also shown to relocalize to the granules upon stress. Here, we investigated the role of stress-induced satellite III transcripts in the relocalization of splicing factors to the granules. We show that the recruitment of the two serine/arginine-rich (SR) proteins SF2/ASF and SRp30c requires the presence of stress-induced satellite III transcripts. In agreement with these findings, we identified the second RNA-recognition motif (RRM2) of hSF2/ASF as the motif required for the targeting to the granules, and we showed by immunoprecipitation that the endogenous hSF2/ASF protein is present in a complex with satellite III transcripts in stressed cells in vivo. Interestingly, satellite III transcripts also immunoprecipitate together with small nuclear ribonucleoproteins (snRNPs) in vivo whereas the intronless hsp70 transcripts do not, supporting the proposal that these transcripts are subject to splicing. Altogether, these data highlight the central role for satellite III transcripts in the targeting and/or retention of splicing factors into the granules upon stress.

Published
2004
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3. Analysis of co-transcriptional RNA processing by RNA-ChIP assay

Author

Bittencourt , Danielle, Auboeuf , Didier, Centre de Recherche en Cancérologie de Lyon (UNICANCER/CRCL), Centre Léon Bérard [Lyon]-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Equipe 7, Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Léon Bérard [Lyon]-Université Claude Bernard Lyon 1 (UCBL), Centre de Recherche en Cancérologie de Lyon ( CRCL ), Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-Centre Léon Bérard [Lyon]-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), and Université de Lyon-Université de Lyon-Centre Léon Bérard [Lyon]-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Claude Bernard Lyon 1 ( UCBL )

Subjects
MESH: Chromatin Immunoprecipitation, Chromatin Immunoprecipitation, MESH: Humans, RNA Splicing, MESH : Humans, MESH: Polymerase Chain Reaction, [SDV.CAN]Life Sciences [q-bio]/Cancer, Polymerase Chain Reaction, [ SDV.CAN ] Life Sciences [q-bio]/Cancer, MESH: RNA Polymerase II, MESH : Chromatin Immunoprecipitation, MESH: RNA, MESH : RNA, Animals, Humans, RNA, MESH: Animals, RNA Polymerase II, MESH : Animals, MESH : RNA Polymerase II, MESH : RNA Splicing, MESH: RNA Splicing, MESH : Polymerase Chain Reaction
Abstract

International audience; It was initially assumed that RNA biogenesis and processing were two independent processes with transcripts undergoing splicing only after being completely synthesized and released from the DNA template. However, transcription and splicing are tightly linked and increasing evidence shows that nascent transcripts can undergo splicing in the vicinity of chromatin while still attached to the RNA polymerase II (RNAPII) transcriptional machinery. These co-transcriptionally spliced RNA molecules are very labile due to dynamic processing and represent a minor subpopulation among total cellular RNA species. Thus, it is difficult to isolate these RNAs in order to study the dynamics and mechanisms of co-transcriptional RNA splicing. To overcome this problem, the RNA-chromatin immunoprecipitation (ChIP) assay, adapted from classical ChIP, allows to co-purify and isolate nascent RNAs after immunoprecipitation of RNAPII. Thanks to this technique, we have shown that co-transcriptional RNA splicing occurs with distinct efficiencies for different genes and different exons of a given transcript and can represent a rate-limiting step in the biological response of messenger RNA synthesis to extracellular stimuli and drug treatments.

Published
2012
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4. CC2D2A mutations in Meckel and Joubert syndromes indicate a genotype-phenotype correlation

Author

Ali Saad, Raymonde Bouvier, S. Romano, Nadia Elkhartoufi, Sophie Audollent, Anne Lise Delezoide, Sophie Saunier, Tania Attié-Bitach, Sophie Patrier, Nathalie Boddaert, Candice Babarit, Rémi Salomon, Jelena Martinovic, Marie Pierre Cordier, Enza Maria Valente, Chantal Esculpavit, Emmanuelle Szenker, Estelle Escudier, Soumaya Mougou-Zerelli, Marie Claire Gubler, Marie Gonzales, Michel Vekemans, Férechté Encha-Razavi, Arnold Munnich, Jeanne Amiel, Joelle Roume, Sylvie Odent, Philippe Loget, Marion Gérard, B. Leheup, Suonavy Khung, Sophie Thomas, Génétique et épigénétique des maladies métaboliques, neurosensorielles et du développement (Inserm U781), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de Cytogénétique, Génétique moléculaire et Biologie de la reproduction, Hôpital Farhat Hached, Service de Génétique Médicale [CHU Necker], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-CHU Necker - Enfants Malades [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Service de pédiatrie générale [CHU Necker], Neuropathies héréditaires et rein en développement, Institut National de la Santé et de la Recherche Médicale (INSERM), CHU Trousseau [APHP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), Physiopathologie des maladies génétiques d'expression pédiatrique, Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de Médecine Infantile III et Génétique Clinique [CHRU Nancy], Centre Hospitalier Régional Universitaire de Nancy (CHRU Nancy), Cabinet d'Anatomie et Cytologie Pathologiques Richier, Service de génétique clinique [Rennes], Université de Rennes (UR)-CHU Pontchaillou [Rennes]-hôpital Sud, Service de génétique médicale, CHI Poissy-Saint-Germain, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Robert Debré-Université Paris Diderot - Paris 7 (UPD7), Service de Biologie du Développement, Service de Génétique, Hospices Civils de Lyon (HCL), Centre de pathologie Est, Service de radiologie pédiatrique [CHU Necker], Imagerie Cerebrale en Psychiatrie, Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Istituto CSS Mendel [Rome, Italy], Department of Medical and Surgical Pediatrics, University Hospital, Messina, French National Research Agency (ANR) : ANR-06-MRAR-034-02United States Department of Health & Human Services National Institutes of Health (NIH) - USA : NS039818-07Fondazione Telethon : GGP08145INSERM-Direction generale de la recherche scientifique et de la renovation technologique (DGRSRT) : CS/RN/2008 56, CS/RN/2008 87, Génétique et épigénétique des maladies métaboliques, neurosensorielles et du développement ( Inserm U781 ), Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Assistance publique - Hôpitaux de Paris (AP-HP)-CHU Necker - Enfants Malades [AP-HP], Institut National de la Santé et de la Recherche Médicale ( INSERM ), Service de génétique et embryologie médicales [CHU Trousseau], Assistance publique - Hôpitaux de Paris (AP-HP)-CHU Trousseau [APHP], Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université Pierre et Marie Curie - Paris 6 ( UPMC ), Centre Hospitalier Régional Universitaire de Nancy ( CHRU Nancy ), Service de génétique clinique, Hôpital Sud, Assistance publique - Hôpitaux de Paris (AP-HP)-Hôpital Robert Debré-Université Paris Diderot - Paris 7 ( UPD7 ), Hospices Civils de Lyon ( HCL ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Istituto CSS Mendel, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), De Villemeur, Hervé, Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Pierre et Marie Curie - Paris 6 (UPMC), and hôpital Sud

Subjects
Male, TMEM67, MESH : Genotype, [SDV.GEN] Life Sciences [q-bio]/Genetics, Ciliopathies, MESH : Syndrome, Cohort Studies, MESH : Proteins, MESH: Genotype, 0302 clinical medicine, MESH: Gene Expression Regulation, Developmental, Missense mutation, Developmental, MESH: Syndrome, MESH: Proteins, MESH: Cohort Studies, [SDV.BDD]Life Sciences [q-bio]/Development Biology, Genetics (clinical), In Situ Hybridization, MESH: Genetic Association Studies, Genetics, 0303 health sciences, Polydactyly, Gene Expression Regulation, Developmental, MESH : In Situ Hybridization, Syndrome, 3. Good health, MESH : Phenotype, Phenotype, RPGRIP1L, MESH : RNA Splicing, MESH : Mutation, MESH: Mutation, Genotype, RNA Splicing, MESH : Male, MESH : Cohort Studies, Genes, Recessive, Biology, CC2D2A, MESH: Phenotype, MESH: Nervous System Diseases, Article, Joubert syndrome, 03 medical and health sciences, MESH: In Situ Hybridization, [SDV.BDD] Life Sciences [q-bio]/Development Biology, medicine, Alleles, Gene Expression Regulation, Genes, Recessive, Genetic Association Studies, Humans, Mutation, Nervous System Diseases, Proteins, [ SDV.BDD ] Life Sciences [q-bio]/Development Biology, MESH: Genes, Recessive, 030304 developmental biology, Meckel-Gruber Syndrome, [SDV.GEN]Life Sciences [q-bio]/Genetics, MESH: Humans, urogenital system, MESH: Alleles, MESH : Humans, MESH : Genes, Recessive, MESH : Nervous System Diseases, MESH : Genetic Association Studies, medicine.disease, MESH: Male, Cytoskeletal Proteins, MESH : Gene Expression Regulation, Developmental, MESH : Alleles, [ SDV.GEN ] Life Sciences [q-bio]/Genetics, MESH: RNA Splicing, 030217 neurology & neurosurgery
Abstract

International audience; Meckel-Gruber syndrome (MKS) is a lethal fetal disorder characterized by diffuse renal cystic dysplasia, polydactyly, a brain malformation that is usually occipital encephalocele, and/or vermian agenesis, with intrahepatic biliary duct proliferation. Joubert syndrome (JBS) is a viable neurological disorder with a characteristic "molar tooth sign" (MTS) on axial images reflecting cerebellar vermian hypoplasia/dysplasia. Both conditions are classified as ciliopathies with an autosomal recessive mode of inheritance. Allelism of MKS and JBS has been reported for TMEM67/MKS3, CEP290/MKS4, and RPGRIP1L/MKS5. Recently, one homozygous splice mutation with a founder effect was reported in the CC2D2A gene in Finnish fetuses with MKS, defining the 6th locus for MKS. Shortly thereafter, CC2D2A mutations were also reported in JBS. The analysis of the CC2D2A gene in our series of MKS fetuses, identified 14 novel truncating mutations in 11 cases. These results confirm the involvement of CC2D2A in MKS and reveal a major contribution of CC2D2A to the disease. We also identified three missense CC2D2A mutations in two JBS cases. Therefore, and in accordance with the data reported regarding RPGRIP1L, our results indicate phenotype-genotype correlations, as missense and presumably hypomorphic mutations lead to JBS while all null alleles lead to MKS.

Published
2009
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5. Bsr, a nuclear-retained RNA with monoallelic expression

Author

Jérôme Cavaillé, Maud Marques, Eugenia Basyuk, Edouard Bertrand, Virginie Marty, Hélène Royo, Laboratoire de biologie moléculaire eucaryote du CNRS ( LBME ), Université Paul Sabatier - Toulouse 3 ( UPS ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de Génomique Fonctionnelle ( IGF ), Centre National de la Recherche Scientifique ( CNRS ) -Université Montpellier 2 - Sciences et Techniques ( UM2 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université Montpellier 1 ( UM1 ) -Université de Montpellier ( UM ), Institut de Génétique Moléculaire de Montpellier ( IGMM ), Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de Biologie du Développement de Marseille ( IBDM ), Aix Marseille Université ( AMU ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Centre de Recherches sur la Cognition Animale [Toulouse] ( CRCA ), Institut de minéralogie et de physique des milieux condensés ( IMPMC ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -IPG PARIS-Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), Departament Geodinàmica i Geofísica, Facultat de Geologia, Laboratoire de Physique Statistique de l'ENS ( LPS ), Fédération de recherche du Département de physique de l'Ecole Normale Supérieure - ENS Paris ( FRDPENS ), Centre National de la Recherche Scientifique ( CNRS ) -École normale supérieure - Paris ( ENS Paris ) -Centre National de la Recherche Scientifique ( CNRS ) -École normale supérieure - Paris ( ENS Paris ) -Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire Colloïdes et Matériaux Divisés ( LCMD ), ESPCI ParisTech-Centre National de la Recherche Scientifique ( CNRS ), Liquides Ioniques et Interfaces Chargées ( LI2C ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -ESPCI ParisTech-Centre National de la Recherche Scientifique ( CNRS ), Ecole Nationale de la Santé Publique ( ENSP ), École des Hautes Études en Santé Publique [EHESP] ( EHESP ), Centre de recherches Paul Pascal ( CRPP ), Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de biologie moléculaire eucaryote (LBME), Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS), Institut de Génomique Fonctionnelle (IGF), Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique Moléculaire de Montpellier (IGMM), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM), Institut de Biologie du Développement de Marseille (IBDM), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches sur la Cognition Animale (CRCA), Centre de Biologie Intégrative (CBI), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Institut des sciences du cerveau de Toulouse. (ISCT), Université Toulouse - Jean Jaurès (UT2J)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse - Jean Jaurès (UT2J)-CHU Toulouse [Toulouse]-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), Département de biologie [Sherbrooke] (UdeS), Faculté des sciences [Sherbrooke] (UdeS), Université de Sherbrooke (UdeS)-Université de Sherbrooke (UdeS), Laboratoire de Physique Statistique de l'ENS (LPS), Université Paris Diderot - Paris 7 (UPD7)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS)-Fédération de recherche du Département de physique de l'Ecole Normale Supérieure - ENS Paris (FRDPENS), École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS), Laboratoire Colloïdes et Matériaux Divisés (LCMD), Centre National de la Recherche Scientifique (CNRS)-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL), Liquides Ioniques et Interfaces Chargées (LI2C), Université Pierre et Marie Curie - Paris 6 (UPMC)-Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris), Ecole Nationale de la Santé Publique (ENSP), École des Hautes Études en Santé Publique [EHESP] (EHESP), Centre de recherches Paul Pascal (CRPP), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches sur la Cognition Animale - UMR5169 (CRCA), Institut des sciences du cerveau de Toulouse. (ISCT), Université Toulouse - Jean Jaurès (UT2J), Université de Toulouse (UT)-Université de Toulouse (UT)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Toulouse - Jean Jaurès (UT2J), Université de Toulouse (UT)-Centre Hospitalier Universitaire de Toulouse (CHU Toulouse)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Fédération de recherche du Département de physique de l'Ecole Normale Supérieure - ENS Paris (FRDPENS), École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), and Ecole Superieure de Physique et de Chimie Industrielles de la Ville de Paris (ESPCI Paris)

Subjects
MESH: Hydroxamic Acids, RNA, Untranslated, MESH : RNA, Messenger, MESH: Introns, RNA Stability, Hydroxamic Acids, RNA Transport, MESH: RNA, Untranslated, 0302 clinical medicine, MESH: RNA Transport, Transcription (biology), Gene cluster, MESH : RNA, MESH: Animals, MESH : Cell Nucleus Structures, MESH : Female, MESH : RNA Transport, Genetics, 0303 health sciences, MESH : Cell Nucleus, MESH : Rats, MESH: RNA Stability, Articles, MESH : RNA Stability, Non-coding RNA, medicine.anatomical_structure, RNA splicing, Female, MESH : RNA Splicing, MESH: Cell Nucleus, MESH : RNA, Untranslated, MESH: Rats, RNA Splicing, MESH: Cytoplasmic Granules, Biology, Cytoplasmic Granules, MESH : Rats, Wistar, MESH : Introns, 03 medical and health sciences, MESH: RNA, MESH : Fibroblasts, medicine, Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Cell Nucleus Structures, RNA, Messenger, Rats, Wistar, Molecular Biology, Gene, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Alleles, MESH: RNA, Messenger, 030304 developmental biology, Cell Nucleus, MESH : Hydroxamic Acids, MESH: Alleles, MESH : Cytoplasmic Granules, Intron, RNA, MESH: Rats, Wistar, Cell Biology, Fibroblasts, Cell Nucleus Structures, Introns, Rats, Cell nucleus, MESH: Fibroblasts, MESH : Animals, MESH: RNA Splicing, MESH : Alleles, MESH: Female, 030217 neurology & neurosurgery
Abstract

The imprinted Dlk1-Gtl2 and Prader-Willi syndrome (PWS) regions are characterized by a complex noncoding transcription unit spanning arrays of tandemly repeated C/D RNA genes. These noncoding RNAs (ncRNAs) are thought to play an essential but still poorly understood role. To better understand the intracellular fate of these large ncRNAs, fluorescence in situ hybridization was carried out at the rat Dlk1-Gtl2 domain. This locus contains a ∼100-kb-long gene cluster comprising 86 homologous RBII-36 C/D RNA gene copies, all of them intron-encoded within the ncRNA gene Bsr. Here, we demonstrate that the Bsr gene is monoallelically expressed in primary rat embryonic fibroblasts as well as in hypothalamic neurons and yields a large amount of unspliced and spliced RNAs at the transcription site, mostly as elongated RNA signals. Surprisingly, spliced Bsr RNAs released from the transcription site mainly concentrate as numerous, stable nuclear foci that do not colocalize with any known subnuclear structures. On drug treatments, a fraction of Bsr RNA relocalizes to the cytoplasm and associates with stress granules (SGs), but not with P-bodies, pointing to a potential link between SGs and the metabolism of ncRNA. Thus, Bsr might represent a novel type of nuclear-retained transcript.

Published
2007
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6. Preferential coupling between dopamine D2 receptors and G-proteins

Author

Jean-Pierre Montmayeur, Janique Guiramand, Emiliana Borrelli, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Neurobiologie de l'audition-plasticité synaptique, Institut National de la Santé et de la Recherche Médicale (INSERM), Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM), Centre des Sciences du Goût et de l'Alimentation [Dijon] ( CSGA ), Institut National de la Recherche Agronomique ( INRA ) -Université de Bourgogne ( UB ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique ( CNRS ), Institut de Génétique et de Biologie Moléculaire et Cellulaire ( IGBMC ), Université de Strasbourg ( UNISTRA ) -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 ), Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] ( IBMM ), and Ecole Nationale Supérieure de Chimie de Montpellier ( ENSCM ) -Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS )

Subjects
MESH: Signal Transduction, MESH : RNA, Messenger, Dopamine, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Messenger, MESH : Adenylate Cyclase, Receptors, Dopamine, Adenylyl cyclase, chemistry.chemical_compound, 0302 clinical medicine, Endocrinology, MESH : 1-Methyl-3-isobutylxanthine, MESH : Tumor Cells, Cultured, 1-Methyl-3-isobutylxanthine, Receptors, Tumor Cells, Cultured, MESH : Receptors, Dopamine, MESH: Receptors, Dopamine, Receptor, MESH : GTP-Binding Proteins, 0303 health sciences, Cultured, ADCY9, MESH: 1-Methyl-3-isobutylxanthine, General Medicine, Tumor Cells, MESH : Forskolin, MESH : Spiperone, Biochemistry, Dopamine receptor, Spiperone, MESH: Spiperone, MESH : RNA Splicing, Signal transduction, MESH : Transfection, MESH: Forskolin, Forskolin, Signal Transduction, Adenylate Cyclase, MESH: GTP-Binding Proteins, MESH : Dopamine, G protein, RNA Splicing, MESH: Dopamine, Biology, Transfection, ADCY10, 03 medical and health sciences, GTP-Binding Proteins, Dopamine receptor D2, MESH: Adenylate Cyclase, Humans, RNA, Messenger, MESH: Tumor Cells, Cultured, Molecular Biology, 030304 developmental biology, MESH: RNA, Messenger, MESH : Signal Transduction, MESH: Humans, MESH: Transfection, Colforsin, MESH : Humans, chemistry, [ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Adenylyl Cyclase Inhibitors, RNA, MESH: RNA Splicing, 030217 neurology & neurosurgery
Abstract

International audience; The D2 dopamine receptor, an inhibitor of adenylyl cyclase, belongs to the family of seven transmembrane domain G-protein-coupled receptors. This receptor is encoded by two mRNAs produced from the same gene by alternative splicing, here referred to as D2L and D2S. The resultant proteins are identical except for an insertion of 29 amino acids in the putative third intracytoplasmic domain. This domain has been shown to be important for the coupling of this family of receptors to G-proteins. We have previously shown that there is differential inhibition of the adenylyl cyclase activity when these two receptors are produced in JEG3 cells; D2S is more efficient than D2L. To understand the molecular basis of such differential activity, we analyzed the G-proteins expressed in these cells. Here we show that G alpha i2 is absent in this cell line. Moreover, it is possible to restore the same inhibitory activity obtained by D2S when an expression vector encoding this alpha-subunit is cotransfected with D2L. In addition, transfections of the two receptors in a recipient cell line containing the three G alpha i subtypes confirm that the two receptors behave similarly. We conclude that the 29-amino acid insertion present in D2L allows it to interact specifically with G alpha i2. These data suggest that in vivo the function of activated D2 receptors is exerted by specific interactions with Gi-protein subtypes.

Published
1993
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