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Self-regulated mechanism of Plk1 localization to kinetochores: lessons from the Plk1-PBIP1 interaction

机译:Plk1本地化到动植物的自我调节机制:来自Plk1-PBIP1相互作用的经验教训

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Mammalian polo-like kinase 1 (Plk1) has been studied extensively as a critical element in regulating various mitotic events during M-phase progression. Plk1 function is spatially regulated through the targeting activity of the conserved polo-box domain (PBD) present in the C-terminal non-catalytic region. Recent progress in our understanding of Plk1 localization to the centromeres shows that Plk1 self-regulates its initial recruitment by phosphorylating a centromeric component PBIP1 and generating its own PBD-binding site. Paradoxically, Plk1 also induces PBIP1 delocalization and degradation from the mitotic kinetochores late in the cell cycle, consequently permitting itself to bind to other kinetochore components. Thus, PBIP1-dependent self-recruitment of Plk1 to the interphase centromeres serves as a prelude to the efficient delivery of Plk1 itself to other kinetochore components whose interactions with Plk1 are vital for proper mitotic progression.
机译:哺乳动物polo样激酶1(Plk1)已被广泛研究作为调节M期进展过程中各种有丝分裂事件的关键因素。 Plk1功能通过C末端非催化区域中存在的保守polo-box域(PBD)的靶向活性在空间上受到调节。我们对Plk1着丝粒定位的了解的最新进展表明,Plk1通过使着丝粒成分PBIP1磷酸化并产生其自身的PBD结合位点来自我调节其初始募集。矛盾的是,Plk1还诱导PBIP1在细胞周期后期从有丝分裂动植物中脱位和降解,因此使其自身能够与其他动线粒结合。因此,Plk1依赖PBIP1的自我招募进入相间着丝粒,是Plk1自身有效传递给其他动粒体组件的序幕,而其他动粒体组件与Plk1的相互作用对于适当的有丝分裂进程至关重要。

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