Poly(ADP-ribose) polymerase 3 (PARP3), a newcomer in cellular response to DNA damage and mitotic progression
| Autor: | Valérie Schreiber, Susan Smith, Laurent Gauthier, Anne Bresson, Denis Biard, François D. Boussin, Christian Boehler, Jean-Michel Saliou, Françoise Dantzer, Sarah Sanglier-Cianférani, Oliver Mortusewicz |
|---|---|
| Přispěvatelé: | Biotechnologie et signalisation cellulaire (BSC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de recherche de l'Ecole de biotechnologie de Strasbourg (IREBS) |
| Rok vydání: | 2011 |
| Předmět: |
Genome instability
MESH: DNA Breaks Double-Stranded Cell Cycle Proteins MESH: Mice Knockout Mass Spectrometry Mice 0302 clinical medicine PARP1 Nuclear Matrix-Associated Proteins DNA Breaks Double-Stranded MESH: Animals MESH: In Situ Hybridization Fluorescence Fluorescent Antibody Technique Indirect In Situ Hybridization Fluorescence Polymerase Mice Knockout Tankyrases 0303 health sciences Microscopy Video Multidisciplinary biology MESH: Genomic Instability Antigens Nuclear Biological Sciences Adenosine Diphosphate Biochemistry 030220 oncology & carcinogenesis ADP-ribosylation Comet Assay Poly(ADP-ribose) Polymerases MESH: Tankyrases MESH: DNA Primers MESH: Cell Line Tumor DNA damage DNA repair Poly ADP ribose polymerase Blotting Western Mitosis MESH: Comet Assay Spindle Apparatus Genomic Instability Colony-Forming Units Assay 03 medical and health sciences MESH: Cell Cycle Proteins Cell Line Tumor Animals Humans Immunoprecipitation MESH: Fluorescent Antibody Technique Indirect MESH: Blotting Western MESH: Colony-Forming Units Assay [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology MESH: Spindle Apparatus MESH: Mice MESH: Antigens Nuclear DNA Primers 030304 developmental biology MESH: Mass Spectrometry MESH: Humans MESH: Adenosine Diphosphate MESH: Immunoprecipitation MESH: Poly(ADP-ribose) Polymerases MESH: Mitosis MESH: Microscopy Video MESH: Nuclear Matrix-Associated Proteins biology.protein |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2011, 108 (7), pp.2783-8. ⟨10.1073/pnas.1016574108⟩ |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.1016574108 |
| Popis: | The ADP ribosyl transferase [poly(ADP-ribose) polymerase] ARTD3(PARP3) is a newly characterized member of the ARTD(PARP) family that catalyzes the reaction of ADP ribosylation, a key posttranslational modification of proteins involved in different signaling pathways from DNA damage to energy metabolism and organismal memory. This enzyme shares high structural similarities with the DNA repair enzymes PARP1 and PARP2 and accordingly has been found to catalyse poly(ADP ribose) synthesis. However, relatively little is known about its in vivo cellular properties. By combining biochemical studies with the generation and characterization of loss-of-function human and mouse models, we describe PARP3 as a newcomer in genome integrity and mitotic progression. We report a particular role of PARP3 in cellular response to double-strand breaks, most likely in concert with PARP1. We identify PARP3 as a critical player in the stabilization of the mitotic spindle and in telomere integrity notably by associating and regulating the mitotic components NuMA and tankyrase 1. Both functions open stimulating prospects for specifically targeting PARP3 in cancer therapy. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|