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.
PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression Available to Purchase
Both authors contributed equally to this work
Both authors contributed equally to this work
Both authors contributed equally to this work
Both authors contributed equally to this work
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; PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression. J Cell Sci 15 April 2003; 116 (8): 1551–1562. doi: https://doi.org/10.1242/jcs.00341
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