Mechanisms of mammalian polo-like kinase 1 (Plk1) localization: Self-priming
Mechanisms of mammalian polo-like kinase 1 (Plk1) localization: Self-priming
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DOI：
10.4161/cc.7.2.5272
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发表时间：
2008-01-15
期刊：
影响因子：
4.3
通讯作者：
Erikson, Raymond L.
中科院分区：
文献类型：
--
作者：
Lee, Kyung S.;Park, Jung-Eun;Erikson, Raymond L.
哺乳动物polo样激酶1（Plk 1）作为调节M期进程中各种有丝分裂事件的关键元件已被深入研究。Plk 1通过C-末端非催化区中存在的保守Polo盒结构域（PBD）的靶向活性进行空间调节。多年来，研究表明PBD形成磷酸化表位结合模块，并且PBD依赖性相互作用对于Plk 1的适当亚细胞定位至关重要。目前流行的模型是PBD结合由Cdc 2或其他Pro定向激酶产生的磷酸表位。在这里，我们讨论了最近的一项发现，Plk 1也自我促进其本地化，产生自己的PBD对接网站。
Mammalian polo-like kinase 1 (Plk1) has been studied intensively as a key element in regulating diverse mitotic events during M-phase progression. Plk1 is spatially regulated through the targeting activity of the conserved polo-box domain (PBD) present in the C-terminal non-catalytic region. Over the years, studies have demonstrated that the PBD forms a phospho-epitope binding module and the PBD-dependent interaction is critical for proper subcellular localization of Plk1. The current prevailing model is that the PBD binds to a phospho-epitope generated by Cdc2 or other Pro-directed kinases. Here we discuss a recent finding that Plk1 also self-promotes its localization by generating its own PBD-docking site.