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First published online 4 March 2003
doi: 10.1242/jcs.00341
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Research Article |
1 Unité 9003 du CNRS, Ecole Supérieure de Biotechnologie de
Strasbourg, Boulevard Sébastien Brant, 67400 Illkirch, France
2 Institut Curie, Section Recherche UMR 144 du CNRS, 26 Rue d'Ulm, F-75248
Paris, France
3 Institut de Biologie Moléculaire des Plantes, CNRS, 12 rue du General
Zimmer, 67084, Strasbourg, France
4 Institut Curie, Section Recherche UMR 147 du CNRS, 26 Rue d'Ulm, F-75248
Paris, France
5 Institut de Génétique et de Biologie Moléculaire et
Cellulaire, CNRS/INSERM/ULP, Collège de France, BP 163, 67400 Illkirch,
France
6 Pharmaceuticals Research, BASF AG, D-67056 Ludwigshafen, Germany
Author for correspondence (e-mail:
demurcia{at}esbs.u-strasbg.fr)
Accepted 2 January 2003
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.
Key words: Centrosome, NAD+ metabolism, DNA damage, G1/S cell cycle control, Midbody
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