Ruan Qin, Wang Qi, Xie Suqing, Fang Yuqiang, Darzynkiewicz Zbigniew, Guan Kunliang, Jhanwar-Uniyal Meena, Dai Wei
Department of Medicine, New York Medical College, Valhalla, NY 10595, USA.
Exp Cell Res. 2004 Mar 10;294(1):51-9. doi: 10.1016/j.yexcr.2003.10.022.
The Golgi apparatus undergoes extensive fragmentation during mitosis in animal cells. Protein kinases play a critical role during fragmentation of the Golgi apparatus. We reported here that Polo-like kinase 3 (Plk3) may be an important mediator during Golgi breakdown. Specifically, Plk3 was concentrated at the Golgi apparatus in HeLa and A549 cells during interphase. At the onset of mitosis, Plk3 signals disintegrated and redistributed in a manner similar to those of Golgi stacks. Nocodazole activated Plk3 kinase activity, correlating with redistribution of Plk3 signals and Golgi fragmentation. In addition, treatment with brefeldin A (BFA), a Golgi-specific poison, also resulted in disappearance of concentrated Plk3 signals. Plk3 interacted with giantin, a Golgi-specific protein. Expression of Plk3, but not the kinase-defective Plk3 (Plk3(K52R)), resulted in significant Golgi breakdown. Given its role in cell cycle progression, Plk3 may be a protein kinase involved in regulation of Golgi fragmentation during the cell cycle.
在动物细胞有丝分裂过程中,高尔基体经历广泛的碎片化。蛋白激酶在高尔基体碎片化过程中起关键作用。我们在此报道,类Polo样激酶3(Plk3)可能是高尔基体解体过程中的一个重要介质。具体而言,在间期,Plk3在HeLa细胞和A549细胞的高尔基体中富集。在有丝分裂开始时,Plk3信号以与高尔基体堆叠解体和重新分布相似的方式解体和重新分布。诺考达唑激活Plk3激酶活性,这与Plk3信号的重新分布和高尔基体碎片化相关。此外,用高尔基体特异性毒素布雷菲德菌素A(BFA)处理也导致Plk3浓缩信号消失。Plk3与高尔基体特异性蛋白巨蛋白相互作用。Plk3的表达,而非激酶缺陷型Plk3(Plk3(K52R))的表达,导致显著的高尔基体解体。鉴于其在细胞周期进程中的作用,Plk3可能是一种参与细胞周期中高尔基体碎片化调控的蛋白激酶。