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首页> 外文期刊>Cell cycle >Glycogen synthase kinase 3 β activity is required for hBora/Aurora A-mediated mitotic entry
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Glycogen synthase kinase 3 β activity is required for hBora/Aurora A-mediated mitotic entry

机译：糖原合酶激酶3β活性是hBora / Aurora A介导的有丝分裂进入所必需的

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摘要

The synthesis and degradation of hBora is important for the regulation of mitotic entry and exist. In G2 phase, hBora can complex with Aurora A to activate Plk1 and control mitotic entry. However, whether the post-translational modification of hBora is relevant to the mitotic entry still unclear. Here, we used the LC-MS/MS phosphopeptide mapping assay to identify 13 in vivo hBora phosphorylation sites and characterized that GSK3β can interact with hBora and phosphorylate hBora at Ser274 and Ser278. Pharmacological inhibitors of GSK3β reduced the retarded migrating band of hBora in cells and diminished the phosphorylation of hBora by in vitro kinase assay. Moreover, as well as in GSK3β activity-inhibited cells, specific knockdown of GSK3β by shRNA and S274A/S278 hBora mutant-expressing cells also exhibited the reduced Plk1 activation and a delay in mitotic entry. It suggests that GSK3β activity is required for hBora-mediated mitotic entry through Ser274 and Ser278 phosphorylation.
机译：hBora的合成和降解对于调节有丝分裂进入至关重要，并且存在。在G2阶段，hBora可以与Aurora A结合以激活Plk1并控制有丝分裂进入。但是，hBora的翻译后修饰是否与有丝分裂进入有关尚不清楚。在这里，我们使用LC-MS / MS磷酸肽图分析法来鉴定13个体内hBora磷酸化位点，并表征GSK3β可以与hBora相互作用并在Ser274和Ser278处磷酸化hBora。通过体外激酶测定，GSK3β的药理抑制剂可降低hBora在细胞中的迁移带延迟，并减少hBora的磷酸化。此外，以及在GSK3β活性抑制细胞中，shRNA和表达S274A / S278 hBora突变体的细胞对GSK3β的特异性敲低也表现出降低的Plk1活化和有丝分裂进入的延迟。这表明，GSK3β活性是hBora介导的通过Ser274和Ser278磷酸化介导的有丝分裂进入所必需的。

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