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JCS ePress online publication date 4 Mar 2003
doi: 10.1242/jcs.00341

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Research Article

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


Angélique Augustin, Catherine Spenlehauer, Hélène Dumond, Josiane Ménissier-de Murcia, Matthieu Piel, Anne-Catherine Schmit, Françoise Apiou, Jean-Luc Vonesch, Michael Kock, Michel Bornens, and Gilbert de Murcia*
* Author for correspondence (e-mail: demurcia{at}esbs.u-strasbg.fr)

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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