SUMOylation regulates the localization and activity of Polo-like kinase 1 during cell cycle in the silkworm, Bombyx mori
SUMOylation regulates the localization and activity of Polo-like kinase 1 during cell cycle in the silkworm, Bombyx mori
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SUMOylation 调节家蚕细胞周期中 Polo 样激酶 1 的定位和活性
DOI：
10.1038/s41598-017-15884-7
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发表时间：
2017-11-14
影响因子：
4.6
通讯作者：
Zhao, Ping
中科院分区：
文献类型：
--
作者：
Li, Zhiqing;Cui, Qixin;Zhao, Ping
Polo-like kinase 1（Plk 1）是一种重要的细胞周期调控因子，在细胞周期中具有特异性的定位和活性。研究表明，Plk 1的磷酸化和泛素化是其自身激活和定位所必需的。在这里，我们报告，SUMO化调节Plk 1在鳞翅目昆虫的家蚕的活性。在没有SUMO化的情况下，它导致Plk 1在中心体和动粒上的定位丢失，以及在中间区的不均匀分布。我们进一步证实了Plk 1的SUMO化位点位于第466位赖氨酸，这是Plk 1定位于中心体所必需的，并且Plk 1的K466突变可能影响其与Smt 3/Ubc 9复合物的相互作用。这些发现也被果蝇波罗和人类Plk 1所证实，它们共同揭示了Plk 1 SUMO化在哺乳动物中的保守作用。此外，Smt 3与Plk 1 SUMO化突变体的结合促进了其在中心体和动粒上的定位，并挽救了内源性Plk 1缺失的细胞中染色体排列的功能缺陷。总之，目前的数据表明，SUMO化的Plk 1可以参与适当的染色体排列和分离在有丝分裂过程中，并提供了一个新的层调控Plk 1的定位和活性在整个细胞周期。
Polo-like kinase 1 (Plk1) is a crucial cell cycle regulator by its specific localization and activity during cell cycle. It has been shown that the phosphorylation and ubiquitylation of Plk1 are required for its own activation and localization. Here, we report that SUMOylation regulates the activity of Plk1 in the lepidopteran insect of Bombyx mori. In the absence of SUMOylation, it causes the lost localization of Plk1 on centrosomes and kinetochores, as well as an uneven distribution in midzone. We further identify that the putative SUMOylation site of Bombyx Plk1 at lysine 466 is required for its localization on centrosomes, and K466 mutation in Plk1 could influence its interaction with Smt3/Ubc9 complex. These findings are also confirmed by Drosophila Polo and human Plk1, which together reveals a conserved role of Plk1 SUMOylation in mammals. Moreover, conjugation of Smt3 to Plk1 SUMOylation mutant promotes its localization on centrosomes and kinetochores, and rescues functional defects of chromosome alignment in cells depleted of endogenous Plk1. Altogether, the present data indicate that the SUMOylation of Plk1 could participate in proper chromosome alignment and segregation during mitosis, and provides a novel layer for the regulation of Plk1 localization and activity throughout cell cycle.