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首页> 外文期刊>Molecular and Cellular Biology >Coordinate Regulation of the Mother Centriole Component Nlp by Nek2 and Plk1 Protein Kinases
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Coordinate Regulation of the Mother Centriole Component Nlp by Nek2 and Plk1 Protein Kinases

机译：Nek2和Plk1蛋白激酶对母亲中心成分Nlp的协调调控。

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Mitotic entry requires a major reorganization of the microtubule cytoskeleton. Nlp, a centrosomal protein that binds γ-tubulin, is a G2/M target of the Plk1 protein kinase. Here, we show that human Nlp and its Xenopus homologue, X-Nlp, are also phosphorylated by the cell cycle-regulated Nek2 kinase. X-Nlp is a 213-kDa mother centriole-specific protein, implicating it in microtubule anchoring. Although constant in abundance throughout the cell cycle, it is displaced from centrosomes upon mitotic entry. Overexpression of active Nek2 or Plk1 causes premature displacement of Nlp from interphase centrosomes. Active Nek2 is also capable of phosphorylating and displacing a mutant form of Nlp that lacks Plk1 phosphorylation sites. Importantly, kinase-inactive Nek2 interferes with Plk1-induced displacement of Nlp from interphase centrosomes and displacement of endogenous Nlp from mitotic spindle poles, while active Nek2 stimulates Plk1 phosphorylation of Nlp in vitro. Unlike Plk1, Nek2 does not prevent association of Nlp with γ-tubulin. Together, these results provide the first example of a protein involved in microtubule organization that is coordinately regulated at the G2/M transition by two centrosomal kinases. We also propose that phosphorylation by Nek2 may prime Nlp for phosphorylation by Plk1.
机译：有丝分裂进入需要微管细胞骨架的重大重组。 Nlp是一种结合γ-微管蛋白的中心体蛋白，是Plk1蛋白激酶的G 2 / M靶标。在这里，我们显示人类Nlp及其非洲爪蟾同源物X-Nlp也被细胞周期调节的Nek2激酶磷酸化。 X-Nlp是一种213 kDa的母体中心蛋白特异性蛋白，与微管锚定有关。尽管在整个细胞周期中其丰度恒定，但在有丝分裂进入时它已从中心体置换。活性Nek2或Plk1的过表达会导致Nlp从相间中心体过早移位。活性Nek2还能够磷酸化和取代缺乏Plk1磷酸化位点的Nlp突变形式。重要的是，激酶非活性Nek2会干扰Plk1诱导的Nlp从相间中心体的置换以及内源性Nlp从有丝分裂纺锤体极的置换，而活性Nek2则在体外刺激Nlp的Plk1磷酸化。与Plk1不同，Nek2不会阻止Nlp与γ-微管蛋白的缔合。总之，这些结果提供了涉及微管组织的蛋白质的第一个例子，该蛋白质在两个 2 / M转换中由两个中心体激酶协同调节。我们还建议，Nek2的磷酸化可能引发Nlp引起Plk1的磷酸化。

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