Phosphorylation of Nlp by Plk1 negatively regulates its dynein-dynactin-dependent targeting to the centrosome
Phosphorylation of Nlp by Plk1 negatively regulates its dynein-dynactin-dependent targeting to the centrosome
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DOI：
10.1242/jcs.02622
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发表时间：
2005-11-01
影响因子：
4
通讯作者：
Nigg, EA
中科院分区：
文献类型：
--
作者：
Casenghi, M;Barr, FA;Nigg, EA
当细胞进入有丝分裂时，微管（MT）网络经历了深刻的重排，部分原因是MT成核和中心体锚定特性的改变。Ninein和Ninein样蛋白（NIp）是间期细胞中参与MT组织的中心体蛋白。我们发现，这两种蛋白质的过度表达诱导高尔基体的碎片，并导致溶酶体向细胞周边分散。NIp和ninein扰乱这些细胞器的细胞质分布的能力取决于它们与动力蛋白-动力肌动蛋白运动复合体相互作用的能力。我们的数据还表明，dynactin是所需的NIp和ninein的中心体的目标。此外，通过polo样激酶1（PIK 1）磷酸化的NIp负调节其与动力肌动蛋白的结合。这些发现揭示了一种机制，通过该机制，PIKI通过控制中心体蛋白的动力蛋白-动力蛋白依赖性转运来帮助协调MT组织的变化与细胞周期进程。
When cells enter mitosis the microtubule (MT) network undergoes a profound rearrangement, in part due to alterations in the MT nucleating and anchoring properties of the centrosome. Ninein and the ninein-like protein (NIp) are centrosomal proteins involved in MT organisation in interphase cells. We show that the overexpression of these two proteins induces the fragmentation of the Golgi, and causes lysosomes to disperse toward the cell periphery. The ability of NIp and ninein to perturb the cytoplasmic distribution of these organelles depends on their ability to interact with the dynein-dynactin motor complex. Our data also indicate that dynactin is required for the targeting of NIp and ninein to the centrosome. Furthermore, phosphorylation of NIp by the polo-like kinase 1 (PIkl) negatively regulates its association with dynactin. These findings uncover a mechanism through which PIkl helps to coordinate changes in MT organisation with cell cycle progression, by controlling the dynein-dynactin-dependent transport of centrosomal proteins.