PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression
PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression
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DOI：
10.1242/jcs.00341
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发表时间：
2003-04-15
影响因子：
4
通讯作者：
de Murcia, G
中科院分区：
文献类型：
--
作者：
Augustin, A;Spenlehauer, C;de Murcia, G
聚（ADP-核糖）聚合酶（PARP）家族的一个新成员，hPARP-3，在这里被确定为中心体的核心组成部分。hPARP-3在整个细胞周期中优先定位于子中心粒。hPARP-3的N端结构域（54个氨基酸）负责其中心体定位。全长hPAPR-3（540个氨基酸，表观质量为67 kDa）在其自动修饰过程中合成ADP-核糖聚合物。过表达hPARP-3或其N端结构域不影响中心体复制或扩增，但干扰G1/S细胞周期进程。PARP-1也存在于中心体的部分细胞周期中，并与hPARP-3相互作用。PARP-1和PARP-3在中心体的存在可能将DNA损伤监测网络与有丝分裂保真度检查点联系起来。
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.