Search

Your search keyword '"MESH: NM23 Nucleoside Diphosphate Kinases"' showing total 3 results
Start Over Descriptor "MESH: NM23 Nucleoside Diphosphate Kinases"
3 results on '"MESH: NM23 Nucleoside Diphosphate Kinases"'

1. Nucleoside diphosphate kinases fuel dynamin superfamily proteins with GTP for membrane remodeling

Author

Ioan Lascu, Graça Raposo, Céline Desbourdes, Philippe Chavrier, Nathalie Sauvonnet, Thibault Lagache, Guillaume Montagnac, Jérôme Guitton, Qinfang Shen, Aurélien Roux, Marie-Lise Lacombe, Maryse Romao, Uwe Schlattner, Lorena Griparic, AlexanderM van der Bliek, Mathieu Boissan, Simona Polo, Institut Curie [Paris], Pathologies biliaires, fibrose et cancer du foie [CHU Saint-Antoine], Centre de Recherche Saint-Antoine (CR Saint-Antoine), Sorbonne Université (SU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Saint-Antoine [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Sorbonne Université (SU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Saint-Antoine [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), Dynamique de la membrane et du cytosquelette, Compartimentation et dynamique cellulaires (CDC), Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), David Geffen School of Medicine [Los Angeles], University of California [Los Angeles] (UCLA), University of California-University of California, Hospices Civils de Lyon (HCL), Université de Lyon, Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Biologie des Interactions Cellulaires (BIC), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Analyse d'images biologiques - Biological Image Analysis (BIA), Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), IFOM, Istituto FIRC di Oncologia Molecolare (IFOM), Università degli Studi di Milano [Milano] (UNIMI), University of Geneva [Switzerland], This work was supported by Institut Curie, CNRS, Fondation ARC pour la Recherche sur le Cancer, Groupement des Entreprises Françaises contre le Cancer, Fondation pour la Recherche Médicale, the Human Frontier Science Program, the Swiss National Fund for Research Grant, and the European Research Council., Pathologies biliaires, fibrose et cancer du foie [CRSA], Centre de Recherche Saint-Antoine (CRSA), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), University of California (UC)-University of California (UC), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Milano = University of Milan (UNIMI), and Université de Genève = University of Geneva (UNIGE)

Subjects
endocrine system, MESH: GTP Phosphohydrolases, GTP', MESH: Mitochondria, [SDV]Life Sciences [q-bio], MESH: Guanosine Diphosphate, Biology, Guanosine triphosphate, MESH: Membrane Fusion, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, MESH: Adenosine Triphosphate, MESH: Animals, Nucleoside Diphosphate Kinase D, 030304 developmental biology, Dynamin, 0303 health sciences, Multidisciplinary, MESH: Guanosine Triphosphate, MESH: Humans, Kinase, Cell biology, MESH: Cell Line, MESH: Dynamins, MESH: Intracellular Membranes, chemistry, Guanosine diphosphate, 030220 oncology & carcinogenesis, ddc:540, MESH: Endocytosis, MESH: Coated Pits, Cell-Membrane, GTP Phosphohydrolases, MESH: NM23 Nucleoside Diphosphate Kinases, MESH: Nucleoside Diphosphate Kinase D, Adenosine triphosphate, MESH: Cell Membrane
Abstract

Supplying power: Right time, right place Cell membranes are very flexible and easily molded to shape; however, to physically pinch off a membrane vesicle from a membrane tube still requires power. A type of molecular machine known as dynamin is involved in this sort of membrane remodeling. Dynamins use guanosine triphosphate (GTP) rather than the more commonly used cellular energy source adenosine triphosphate to work. Boissan et al. now show that two separate dynamins found in the cytoplasm or the mitochondria both use the same sort of enzyme—nucleoside diphosphate kinases—to provide GTP at just the right time and the right place to power membrane fission. Science , this issue p. 1510

Published
2014
Full Text
View/download PDF

2. The nucleoside diphosphate kinase D (NM23-H4) binds the inner mitochondrial membrane with high affinity to cardiolipin and couples nucleotide transfer with respiration

Author

Marie-Lise Lacombe, Christiane Mailleau, Malgorzata Tokarska-Schlattner, Caroline Borot, Oliver Speer, Uwe Schlattner, Mathieu Boissan, Annie Munier, Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre de Recherche Saint-Antoine (UMRS893), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Biologie et Biochimie Cellulaire du Vieillissement, Université Paris Diderot - Paris 7 (UPD7), Department of Biology, Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich)-Institute of Cell Biology, Hamant, Sarah, University of Zurich, and Schlattner, U

Subjects
Male, 1303 Biochemistry, MESH: Sequence Homology, Amino Acid, Mitochondrial intermembrane space, Mitochondria, Liver, MESH: Amino Acid Sequence, Mitochondrion, Biochemistry, 1307 Cell Biology, chemistry.chemical_compound, 0302 clinical medicine, Cardiolipin, MESH: Animals, MESH: Oxygen Consumption, Inner mitochondrial membrane, Nucleoside Diphosphate Kinase D, 0303 health sciences, Peripheral membrane protein, NM23 Nucleoside Diphosphate Kinases, Nucleoside-diphosphate kinase, Mitochondria, Cell biology, Metabolism and Bioenergetics, MESH: Intracellular Membranes, 030220 oncology & carcinogenesis, MESH: Mitochondria, Liver, MESH: Rats, Cardiolipins, MESH: Mitochondria, Molecular Sequence Data, 610 Medicine & health, Biology, 03 medical and health sciences, Oxygen Consumption, 1312 Molecular Biology, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, Humans, Inner membrane, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amino Acid Sequence, Rats, Wistar, Molecular Biology, 030304 developmental biology, MESH: Humans, MESH: Molecular Sequence Data, Sequence Homology, Amino Acid, Intracellular Membranes, MESH: Rats, Wistar, Cell Biology, MESH: Male, Rats, chemistry, 10036 Medical Clinic, MESH: NM23 Nucleoside Diphosphate Kinases, MESH: Cardiolipins
Abstract

International audience; Nucleoside diphosphate kinase (NDPK/Nm23), responsible for intracellular di- and triphosphonucleoside homeostasis, plays multiple roles in cellular energetics, signaling, proliferation, differentiation and tumor invasion. The only human NDPK with a mitochondrial targeting sequence is NDPK-D, the NME4 gene product, which is a peripheral protein of mitochondrial membranes. Subfractionation of rat liver and HEK 293 cell mitochondria revealed that NDPK-D is essentially bound to the inner membrane. Surface plasmon resonance analysis of the interaction using recombinant NDPK-D and model liposomes showed that NDPK-D interacts electrostatically with anionic phospholipids, with highest affinity observed for cardiolipin. Mutation of the central arginine (Arg-90) in a surface-exposed basic RRK motif unique to NDPK-D strongly reduced interaction with anionic phospholipids. Due to its symmetrical hexameric structure, NDPK-D was able to cross-link anionic phospholipid-containing liposomes, suggesting that NDPK-D could promote intermembrane contacts. Latency assays with isolated mitochondria and antibody binding to mitoplasts indicated a dual orientation for NDPK-D. In HeLa cells, stable expression of wild type but not of the R90D mutant led to membrane-bound enzyme in vivo. Respiration was significantly stimulated by the NDPK substrate TDP in mitochondria containing wild-type NDPK-D, but not in those expressing the R90D mutant, which is catalytically equally active. This indicates local ADP regeneration in the mitochondrial intermembrane space and a tight functional coupling of NDPK-D with oxidative phosphorylation that depends on its membrane-bound state.

Published
2008
Full Text
View/download PDF

3. Structural and catalytic properties and homology modelling of the human nucleoside diphosphate kinase C, product of the DRnm23 gene

Author

Erent, Muriel, Gonin, Philippe, Cherfils, Jacqueline, Tissier, Pierre, Raschellà, Giuseppe, Giartosio, Anna, Agou, Fabrice, Sarger, Claude, Lacombe, Marie-Lise, Konrad, Manfred, Lascu, Ioan, Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'enzymologie et biochimie structurales (LEBS), Centre National de la Recherche Scientifique (CNRS), Agenzia Nazionale per le nuove Tecnologie, l’energia e lo sviluppo economico sostenibile (ENEA), Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP), Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Régulation Enzymatique des Activités Cellulaires, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM), CHU Saint-Antoine [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), Max-Planck-Institut für Biophysikalische Chemie - Max Planck Institute for Biophysical Chemistry [Göttingen], Max-Planck-Gesellschaft, This work was supported in part by a fellowship from the Association pour la Recherche contre le Cancer (grant 9633 to I. L. and fellowships to M. E. and to P. G.) and by a PROCOPE programme (1995±1997)., Agenzia Nazionale per le nuove Tecnologie, l’energia e lo sviluppo economico sostenibile = Italian National Agency for New Technologies, Energy and Sustainable Economic Development (ENEA), Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome] (UNIROMA), and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, MESH: Enzyme Stability, Protein Denaturation, Hot Temperature, MESH: Sequence Homology, Amino Acid, [SDV]Life Sciences [q-bio], Blotting, Western, Molecular Sequence Data, MESH: Sequence Alignment, MESH: Amino Acid Sequence, MESH: Monomeric GTP-Binding Proteins, MESH: Hot Temperature, Catalysis, Neuroblastoma, Structure-Activity Relationship, MESH: Structure-Activity Relationship, Enzyme Stability, Tumor Cells, Cultured, MESH: Blotting, Western, Humans, Urea, MESH: Tumor Cells, Cultured, Amino Acid Sequence, MESH: Urea, Monomeric GTP-Binding Proteins, MESH: Humans, MESH: Molecular Sequence Data, hybrid, Sequence Homology, Amino Acid, nucleoside diphosphate kinase, oligomeric proteins, MESH: Transcription Factors, NM23 Nucleoside Diphosphate Kinases, MESH: Catalysis, Drnm23, MESH: Neuroblastoma, Isoenzymes, protein stability, Nucleoside-Diphosphate Kinase, MESH: Isoenzymes, MESH: NM23 Nucleoside Diphosphate Kinases, MESH: Protein Denaturation, Sequence Alignment, MESH: Nucleoside-Diphosphate Kinase, MESH: Models, Molecular, Transcription Factors
Abstract

International audience; The human DRnm23 gene was identified by differential screening of a cDNA library obtained from chronic myeloid leukaemia-blast crisis primary cells. The over-expression of this gene inhibits differentiation and induces the apoptosis of myeloid precursor cell lines. We overproduced in bacteria a truncated form of the encoded protein lacking the first 17 N-terminal amino acids. This truncated protein was called nucleoside diphosphate (NDP) kinase CDelta. NDP kinase CDelta had similar kinetic properties to the major human NDP kinases A and B, but was significantly more stable to denaturation by urea and heat. Analysis of denaturation by urea, using size exclusion chromatography, indicated unfolding without the dissociation of subunits, whereas renaturation occurred via a folded monomer. The stability of the protein depended primarily on subunit interactions. Homology modelling of the structure of NDP kinase CDelta, based on the crystal structure of NDP kinase B, indicated that NDP kinase CDelta had several additional stabilizing interactions. The overall structure of the two enzymes appears to be identical because NDP kinase CDelta readily formed mixed hexamers with NDP kinase A. It is possible that mixed hexamers can be observed in vivo.

Published
2001
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results