| PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression. | |
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MedLine Citation:
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PMID: 12640039 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A novel member of the poly(ADP-ribose) polymerase (PARP) family, hPARP-3, is identified here as a core component of the centrosome. hPARP-3 is preferentially localized to the daughter centriole throughout the cell cycle. The N-terminal domain (54 amino acids) of hPARP-3 is responsible for its centrosomal localization. Full-length hPAPR-3 (540 amino acids, with an apparent mass of 67 kDa) synthesizes ADP-ribose polymers during its automodification. Overexpression of hPARP-3 or its N-terminal domain does not influence centrosomal duplication or amplification but interferes with the G1/S cell cycle progression. PARP-1 also resides for part of the cell cycle in the centrosome and interacts with hPARP-3. The presence of both PARP-1 and PARP-3 at the centrosome may link the DNA damage surveillance network to the mitotic fidelity checkpoint. |
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Authors:
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Angélique Augustin; Catherine Spenlehauer; Hélène Dumond; Josiane Ménissier-De Murcia; Matthieu Piel; Anne-Catherine Schmit; Françoise Apiou; Jean-Luc Vonesch; Michael Kock; Michel Bornens; Gilbert De Murcia |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of cell science Volume: 116 ISSN: 0021-9533 ISO Abbreviation: J. Cell. Sci. Publication Date: 2003 Apr |
Date Detail:
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Created Date: 2003-03-17 Completed Date: 2004-01-30 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0052457 Medline TA: J Cell Sci Country: England |
Other Details:
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Languages: eng Pagination: 1551-62 Citation Subset: IM |
Affiliation:
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Unité 9003 du CNRS, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant, 67400 Illkirch, France. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/AY126341 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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3T3 Cells Amino Acid Sequence Animals Base Sequence CHO Cells Cell Cycle Proteins / genetics, metabolism* Cell Division / drug effects Cell Line Cell Survival / drug effects, genetics Centrioles / metabolism* Cricetinae G1 Phase / drug effects Hela Cells Humans Hydroxyurea / pharmacology In Situ Hybridization, Fluorescence / methods Mice Molecular Sequence Data Poly(ADP-ribose) Polymerases / antagonists & inhibitors, genetics, metabolism* S Phase / drug effects Sequence Alignment Sequence Homology, Amino Acid |
| Chemical | |
Reg. No./Substance:
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0/Cell Cycle Proteins; 127-07-1/Hydroxyurea; EC 2.4.2.30/PARP3 protein, human; EC 2.4.2.30/Poly(ADP-ribose) Polymerases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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