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First published online 4 March 2003
doi: 10.1242/jcs.00341

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PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression

Angélique Augustin^1,*, Catherine Spenlehauer^1,*, Hélène Dumond¹, Josiane Ménissier-de Murcia¹, Matthieu Piel², Anne-Catherine Schmit³, Françoise Apiou⁴, Jean-Luc Vonesch⁵, Michael Kock⁶, Michel Bornens² and Gilbert de Murcia^1,

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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