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Your search keyword '"MESH : Protein Stability"' showing total 3 results
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3 results on '"MESH : Protein Stability"'

1. Conserved structure and domain organization among bacterial Slc26 transporters

Author

Martine Moulin, Arnaud Javelle, Heather E. Findlay, Emma L R Compton, David Norman, Michael Haertlein, Kimberly Page, Ulrich Zachariae, Frank Gabel, Lujan Center for Neutron Scattering, LANL, Los Alamos National Laboratory ( LANL ), School of Biochemistry, University of Bristol [Bristol], Unité de recherche Géosciences Marines (Ifremer) ( GM ), Institut Français de Recherche pour l'Exploitation de la Mer ( IFREMER ), Institut de biologie structurale ( IBS - UMR 5075 ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Grenoble Alpes ( UGA ), Institut national d’études supérieures agronomiques de Montpellier ( Montpellier SupAgro ), Los Alamos National Laboratory (LANL), Unité de recherche Géosciences Marines (Ifremer) (GM), Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER), Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Thomas, Frank, Géosciences Marines (GM), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
Models, Molecular, MESH : Molecular Sequence Data, MESH: Yersinia enterocolitica, Biochemistry, Conserved sequence, MESH: Protein Structure, Tertiary, 0302 clinical medicine, MESH : Scattering, Small Angle, MESH : Protein Stability, MESH : Bacterial Proteins, MESH: Phylogeny, MESH: Bacterial Proteins, Conserved Sequence, Phylogeny, 0303 health sciences, MESH: Conserved Sequence, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Protein Stability, MESH: Anion Transport Proteins, MESH : Yersinia enterocolitica, Transmembrane protein, Transport protein, MESH : Protein Structure, Tertiary, MESH: Models, Molecular, Protein family, [SDV.BBM.BS] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], MESH : Models, Molecular, Protein domain, Anion Transport Proteins, Molecular Sequence Data, Biology, RS, 03 medical and health sciences, Bacterial Proteins, Phylogenetics, MESH : Conserved Sequence, MESH: Protein Stability, Scattering, Small Angle, Humans, MESH : Bacteria, Homology modeling, Molecular Biology, MESH: Scattering, Small Angle, 030304 developmental biology, Yersinia enterocolitica, MESH: Humans, MESH: Molecular Sequence Data, Bacteria, MESH : Humans, MESH : Phylogeny, Cell Biology, Protein Structure, Tertiary, MESH: Bacteria, MESH : Anion Transport Proteins, 030217 neurology & neurosurgery, Function (biology), [ SDV.BBM.BS ] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
Abstract

International audience; The Slc26 proteins are a ubiquitous superfamily of anion transporters conserved from bacteria to humans, among which four have been identified as human disease genes. Our functional knowledge of this protein family has increased but limited structural information is available. These proteins contain a transmembrane (TM) domain and a C-terminal cytoplasmic sulfate transporter and anti-sigma factor (STAS) domain. In a fundamental step towards understanding the structure/function relationships within the family we have used small-angle neutron scattering (SANS) on two distantly related bacterial homologues to show that there is a common, dimeric and structural architecture among Slc26A transporters. Pulsed electron-electron double resonance (PELDOR) spectroscopy supports the dimeric SANS-derived model. Using chimaeric/truncated proteins we have determined the domain organization: the STAS domains project away from the TM core and are essential for protein stability. We use the SANS-generated envelopes to assess a homology model of the TM core.

Published
2014

2. The PKCθ pathway participates in the aberrant accumulation of Fra-1 protein in invasive ER-negative breast cancer cells. : PKCθ pathway stabilises Fra-1

Author

Belguise, Karine, Milord, Sandrine, Galtier, Florence, Moquet-Torcy, Gabriel, Piechaczyk, Marc, Chalbos, Dany, Institut de recherche en cancérologie de Montpellier ( IRCM ), Université Montpellier 1 ( UM1 ) -CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université de Montpellier ( UM ), Institut de Génétique Moléculaire de Montpellier ( IGMM ), Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), This work was supported by the ' Institut National de la Santé et de la Recherche Médicale ', the University of Montpellier 1, the ' Ligue Nationale Contre le Cancer-comité de l'Hérault ', the ' Association pour la Recherche sur le Cancer ' (fellowship to K. Belguise) and the French 'Ministère de la Recherche et de l'Enseignement Supérieur' (fellowship to S. Milord). M. Piechaczyk's laboratory was supported as an ' Equipe Labellisée ' of the ' Ligue Nationale Contre le Cancer '., Institut de recherche en cancérologie de Montpellier (IRCM - U896 Inserm - UM1), Université Montpellier 1 (UM1)-CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Institut de Génétique Moléculaire de Montpellier (IGMM), and Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)

Subjects
MESH : Protein-Serine-Threonine Kinases, MESH: Cell Line, Tumor, MESH : MAP Kinase Signaling System, [SDV.CAN]Life Sciences [q-bio]/Cancer, MESH : Breast Neoplasms, MESH: Protein-Serine-Threonine Kinases, [ SDV.CAN ] Life Sciences [q-bio]/Cancer, MESH : Phosphorylation, MESH: Protein Stability, MESH : Protein Stability, MESH : Cell Movement, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH : Female, MESH : Protein Kinase C, MESH: Cell Movement, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH : Protein Processing, Post-Translational, MESH : Isoenzymes, MESH: Humans, MESH: Phosphorylation, MESH: Proto-Oncogene Proteins c-fos, MESH: MAP Kinase Signaling System, MESH : Cell Line, Tumor, MESH : Humans, MESH: Protein Kinase C, MESH : Proto-Oncogene Proteins c-fos, MESH: Protein Processing, Post-Translational, MESH: Isoenzymes, MESH: Receptors, Estrogen, MESH : Receptors, Estrogen, MESH: Female, MESH: Breast Neoplasms
Abstract

International audience; Fra-1 is aberrantly expressed in a large number of cancer cells and tissues, and emerging evidence suggests an important role for this Fos family protein in both oncogenesis and the progression or maintenance of many tumour types. Here, we show that the concentration of Fra-1 is high in invasive oestrogen receptor (ER)-negative (ER-) breast cancer cell lines, regardless of their Ras pathway status. All of the ER- cells express high levels of activated PKCθ, and the inhibition of PKCθ activity using RNA interference or the expression of a dominant-negative mutant results in a dramatic reduction in Fra-1 abundance. Conversely, the ectopic expression of constitutively active PKCθ leads to Fra-1 phosphorylation and accumulation in poorly invasive ER+ cells. This accumulation is due to the stabilisation of the Fra-1 protein through PKCθ signalling, whereas other members of the PKC family are ineffective. Both Ste20-related proline-alanine-rich kinase (SPAK) and ERK1/2, whose activities are upregulated by PKCθ, participate in PKCθ-driven Fra-1 stabilisation. Interestingly, their relative contributions appear to be different depending on the cell line studied. ERK1/2 signalling has a major role in ER- MDA-MB-231 cells, whereas Fra-1 accumulation occurs mainly through SPAK signalling in ER- BT549 cells. Fra-1 mutational analysis shows that the phosphorylation of S265, T223 and T230 is critical for PKCθ-driven Fra-1 stabilisation. Phosphorylation of the protein was confirmed using specific antisera against Fra-1 phosphorylated on T223 or S265. In addition, Fra-1 participates in PKCθ-induced cell invasion and is necessary for PKCθ-induced cell migration. In summary, we identified PKCθ signalling as an important regulator of Fra-1 accumulation in ER- breast cancer cells. Moreover, our results suggest that PKCθ could participate in progression of some breast cancers and could be a new therapeutic target.

Published
2012
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3. Live-Cell Imaging Reveals Multiple Interactions between Epstein-Barr Virus Nuclear Antigen 1 and Cellular Chromatin during Interphase and Mitosis

Author

Maïté Coppey-Moisan, Tristan Piolot, Vincent Maréchal, Gabriel Dos Reis, Christophe Klein, Nathalie Jourdan, Marc Tramier, Frédérique Quignon, Aude Jobart-Malfait, Adaptation Biologique et Vieillissement = Biological Adaptation and Ageing (B2A), 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), 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), Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche des Cordeliers (CRC (UMR_S 872)), Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et Développement de Rennes (IGDR), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Centre de Recherche des Cordeliers ( CRC (UMR_S 872) ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Institut Jacques Monod ( IJM ), Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de Génétique et Développement de Rennes ( IGDR ), Université de Rennes 1 ( UR1 ), Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -Centre National de la Recherche Scientifique ( CNRS ) -Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), UPMC, INSERM, Université Paris Descartes - Paris 5 (UPD5)-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), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), and De Villemeur, Hervé

Subjects
MESH : Cell Line, viruses, [SDV]Life Sciences [q-bio], Gene Expression, MESH : Hepatocytes, MESH: Hepatocytes, Chromatin bridge, 0302 clinical medicine, MESH : Protein Transport, hemic and lymphatic diseases, MESH : Protein Stability, 0303 health sciences, MESH : Chromatin, MESH : Epstein-Barr Virus Nuclear Antigens, MESH : Interphase, Protein Stability, RNA-Binding Proteins, MESH : Protein Binding, Cell cycle, MESH : Mitosis, Chromatin, Virus-Cell Interactions, Protein Transport, 030220 oncology & carcinogenesis, Premature chromosome condensation, Interphase, MESH: Cell Nucleolus, MESH : Carrier Proteins, MESH: Epstein-Barr Virus Nuclear Antigens, Cell Nucleolus, Plasmids, Protein Binding, MESH: Protein Transport, MESH: Gene Expression, Immunology, Mitosis, MESH: Carrier Proteins, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Microbiology, Cell Line, MESH: Chromatin, MESH: Interphase, 03 medical and health sciences, G2 phase, Prophase, MESH: Plasmids, MESH: Protein Stability, Virology, MESH: HMGB2 Protein, HMGB2 Protein, Humans, MESH: Protein Binding, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, 030304 developmental biology, MESH: Humans, [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology, MESH : Humans, MESH: Mitosis, MESH : HMGB2 Protein, Molecular biology, MESH: Cell Line, MESH : Gene Expression, Epstein-Barr Virus Nuclear Antigens, MESH : Plasmids, Insect Science, MESH : Cell Nucleolus, Hepatocytes, Carrier Proteins
Abstract

Epstein-Barr virus (EBV) establishes a life-long latent infection in humans. In proliferating latently infected cells, EBV genomes persist as multiple episomes that undergo one DNA replication event per cell cycle and remain attached to the mitotic chromosomes. EBV nuclear antigen 1 (EBNA-1) binding to the episome and cellular genome is essential to ensure proper episome replication and segregation. However, the nature and regulation of EBNA-1 interaction with chromatin has not been clearly elucidated. This activity has been suggested to involve EBNA-1 binding to DNA, duplex RNA, and/or proteins. EBNA-1 binding protein 2 (EBP2), a nucleolar protein, has been proposed to act as a docking protein for EBNA-1 on mitotic chromosomes. However, there is no direct evidence thus far for EBP2 being associated with EBNA-1 during mitosis. By combining video microscopy and Förster resonance energy transfer (FRET) microscopy, we demonstrate here for the first time that EBNA-1 and EBP2 interact in the nucleoplasm, as well as in the nucleoli during interphase. However, in strong contrast to the current proposed model, we were unable to observe any interaction between EBNA-1 and EBP2 on mitotic chromosomes. We also performed a yeast double-hybrid screening, followed by a FRET analysis, that led us to identify HMGB2 (high-mobility group box 2), a well-known chromatin component, as a new partner for EBNA-1 on chromatin during interphase and mitosis. Although the depletion of HMGB2 partly altered EBNA-1 association with chromatin in HeLa cells during interphase and mitosis, it did not significantly impact the maintenance of EBV episomes in Raji cells.

Published
2012
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