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

被引:121
作者
Augustin, A
Spenlehauer, C
Dumond, H
Murcia, JMD
Piel, M
Schmit, AC
Apiou, F
Vonesch, JL
Kock, M
Bornens, M
de Murcia, G
机构
[1] Ecole Super Biotechnol Strasbourg, Unite 9003, CNRS, F-67400 Illkirch Graffenstaden, France
[2] Inst Curie, Sect Rech, UMR 144, CNRS, F-75248 Paris, France
[3] CNRS, Inst Biol Mol Plantes, F-67084 Strasbourg, France
[4] Inst Curie, Sect Rech, UMR 147, CNRS, F-75248 Paris, France
[5] Coll France, Inst Genet & Biol Mol & Cellulaire, CNRS, INSERM,ULP, F-67400 Illkirch Graffenstaden, France
[6] BASF AG, Pharmaceut Res, D-67056 Ludwigshafen, Germany
关键词
centrosome; NAD(+) metabolism; DNA damage; G1/S cell cycle control; midbody;
D O I
10.1242/jcs.00341
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:1551 / 1562
页数:12
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