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Your search keyword '"Poly Adenosine Diphosphate Ribose/*metabolism"' showing total 2 results
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2 results on '"Poly Adenosine Diphosphate Ribose/*metabolism"'

1. Poly(ADP-ribose): novel functions for an old molecule

Author

Jean-Christophe Amé, Gilbert de Murcia, Valérie Schreiber, Françoise Dantzer, Institut Gilbert-Laustriat : Biomolécules, Biotechnologie, Innovation Thérapeutique, Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Cancérogenèse et mutagenèse moléculaire et structurale (CMMS), Centre National de la Recherche Scientifique (CNRS), and Klotz, Evelyne

Subjects
Models, Molecular, MESH: Cell Death, MESH: Inflammation, Poly Adenosine Diphosphate Ribose, DNA Repair, Cell division, Protein Conformation, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], MESH: Protein Isoforms, Diphtheria Toxin/chemistry, chemistry.chemical_compound, MESH: Protein Conformation, 0302 clinical medicine, PARP1, Models, Protein Isoforms, Diphtheria Toxin, MESH: Animals, Non-U.S. Gov't, MESH: DNA Repair, 0303 health sciences, NAD/biosynthesis, Cell Death, Inflammation/metabolism, Cell Death/physiology, MESH: NAD, MESH: Diphtheria Toxin, Protein Isoforms/chemistry/genetics/*metabolism, Cell biology, Poly Adenosine Diphosphate Ribose/chemistry/genetics/*metabolism, MESH: Poly Adenosine Diphosphate Ribose, Biochemistry, Multigene Family, 030220 oncology & carcinogenesis, MESH: Cell Division, Poly(ADP-ribose) Polymerases, Poly(ADP-ribose) Polymerases/chemistry/genetics/*metabolism, Cell Division, MESH: Models, Molecular, Intracellular, Poly ADP ribose polymerase, Cell Division/physiology, Biology, Research Support, 03 medical and health sciences, Ribose, Animals, Humans, Molecular Biology, Poly(ADP-ribose) glycohydrolase, 030304 developmental biology, Inflammation, MESH: DNA Damage, MESH: Humans, MESH: Poly(ADP-ribose) Polymerases, Molecular, Cell Biology, NAD, Spindle apparatus, chemistry, MESH: Multigene Family, NAD+ kinase, DNA Damage
Abstract

1471-0072 (Print) Journal Article Review; The addition to proteins of the negatively charged polymer of ADP-ribose (PAR), which is synthesized by PAR polymerases (PARPs) from NAD(+), is a unique post-translational modification. It regulates not only cell survival and cell-death programmes, but also an increasing number of other biological functions with which novel members of the PARP family have been associated. These functions include transcriptional regulation, telomere cohesion and mitotic spindle formation during cell division, intracellular trafficking and energy metabolism.

Published
2006
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2. Inhibition of Aurora-B kinase activity by poly(ADP-ribosyl)ation in response to DNA damage

Author

Josiane Ménissier-de Murcia, Lucia Monaco, Gilbert de Murcia, Romain Loury, Ullas Kolthur-Seetharam, Paolo Sassone-Corsi, Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut Gilbert-Laustriat : Biomolécules, Biotechnologie, Innovation Thérapeutique, Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), and Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Louis Pasteur - Strasbourg I

Subjects
Poly Adenosine Diphosphate Ribose, Histones/metabolism, Poly (ADP-Ribose) Polymerase-1, Proteins/*metabolism, Histones, Mice, 0302 clinical medicine, Aurora Kinases, Chlorocebus aethiops, Aurora Kinase B, MESH: Animals, MESH: Proteins, Phosphorylation, Non-U.S. Gov't, DNA-PKcs, Aurora Kinase A, MESH: Histones, 0303 health sciences, Multidisciplinary, histone h3, mitosis, phosphorylation, poly(adp-ribose) polymerase-1, biology, Poly Adenosine Diphosphate Ribose/*metabolism, Blotting, Biological Sciences, MESH: COS Cells, MESH: Poly Adenosine Diphosphate Ribose, 030220 oncology & carcinogenesis, COS Cells, Protein-Serine-Threonine Kinases/*metabolism, Casein kinase 2, Poly(ADP-ribose) Polymerases, Western, DNA damage, DNA repair, Blotting, Western, Protein Serine-Threonine Kinases, Research Support, MESH: Protein-Serine-Threonine Kinases, Cercopithecus aethiops, 03 medical and health sciences, Animals, Immunoprecipitation, MESH: Blotting, Western, Comparative Study, CHEK1, Kinase activity, MESH: Mice, 030304 developmental biology, MESH: DNA Damage, MESH: Phosphorylation, MESH: Immunoprecipitation, Cyclin-dependent kinase 2, MESH: Poly(ADP-ribose) Polymerases, Proteins, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, Molecular biology, MESH: Cercopithecus aethiops, Poly(ADP-ribose) Polymerases/*metabolism, biology.protein, NIH 3T3 Cells, Cyclin-dependent kinase 9, DNA Damage, MESH: NIH 3T3 Cells
Abstract

The cell cycle-regulated Aurora-B kinase is a chromosomal passenger protein that is implicated in fundamental mitotic events, including chromosome alignment and segregation and spindle checkpoint function. Aurora-B phosphorylates serine 10 of histone H3, a function that has been associated with mitotic chromatin condensation. We find that activation of poly(ADP-ribose) polymerase (PARP) 1 by DNA damage results in a rapid block of H3 phosphorylation. PARP-1 is a NAD + -dependent enzyme that plays a multifunctional role in DNA damage detection and repair and maintenance of genomic stability. Here, we show that Aurora-B physically and specifically associates with the BRCT (BRCA-1 C-terminal) domain of PARP-1. Aurora-B becomes highly poly(ADP-ribosyl)ated in response to DNA damage, a modification that leads to a striking inhibition of its kinase activity. The highly similar Aurora-A kinase is not regulated by PARP-1. We propose that the specific inhibition of Aurora-B kinase activity by PARP-1 contributes to the physiological response to DNA damage.

Published
2005
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