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首页> 外文期刊>Cell cycle >A tension-independent mechanism reduces Aurora B-mediated phosphorylation upon microtubule capture by CENP-E at the kinetochore
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A tension-independent mechanism reduces Aurora B-mediated phosphorylation upon microtubule capture by CENP-E at the kinetochore

机译：张力无关的机制通过CENP-E在KINETOCHORE上通过CENP-E捕获时减少了极其B介导的磷酸化

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摘要

During mitosis, Aurora B kinase is required for forming proper bi-oriented kinetochore-microtubule attachments. Current models suggest that tension exerted between a pair of sister-kinetochores (inter-kinetochore stretch) produces a spatial separation of Aurora B kinase from kinetochore-associated microtubule binding substrates, such as the Knl1-Mis12-Ndc80 (KMN) network, resulting in a decrease of phosphorylation and, thus, an increase of affinity for microtubules. Using Single-Molecule High-Resolution Colocalization (SHREC) microscopy analysis of the kinetochore-associated motor CENP-E, we now show that CENP-E undergoes structural rearrangements prior to and after tension generation at the kinetochore, and displays a bi-modal Gaussian distribution on a pair of bi-oriented sister kinetochores. The conformational change of CENP-E depends on its microtubule-stimulated motor motility and the highly flexible coiled-coil between its motor and kinetochore-binding tail domains. Chemical inhibition of the motor motility or perturbations of the coiled-coil domain of CENP-E increases Aurora B-mediated Ndc80 phosphorylation in a tension-independent manner. Metaphase chromosome misalignment caused by CENP-E inhibition can be rescued by chemical inhibition of Aurora B kinase. Furthermore, a pair of monotelic sister-kinetochores shows asymmetric levels of Aurora B-mediated phosphorylation in mono-polar spindles depending on CENP-E motor activity. These results collectively suggest a tension-independent mechanism to reduce Aurora B-mediated phosphorylation of outer kinetochore components in response to microtubule capture by CENP-E. ? 2019, ? 2019 Informa UK Limited, trading as Taylor & Francis Group.
机译：在有丝分裂期间，Aurora B激酶需要形成适当的双向运动学 - 微管附件。目前的模型表明，一对姐妹 - kinetochores（间基因克洛克群岛）之间施加的张力产生了来自Kinetochore相关的微管粘合基材的Aurora B激酶的空间分离，例如KNL1-MIS12-NDC80（KMN）网络，导致磷酸化的减少，因此，对微管的亲和力的增加。使用单分子高分辨率的分层化（SHREC）显微镜分析Kinetochore相关的电动机CENP-E，我们现在表明CENP-E在Kinetochore张力发电之前和之后进行的结构重排，并显示了双模莫斯卡分布在一对双向姐妹Kinetochores。 CENP-E的构象变化取决于其微管刺激的电动机运动和其电动机和动力学结合尾部之间的高度柔性卷绕线圈。 CENP-E的卷轴螺旋域的电动机运动或扰动的化学抑制增加了张紧的方式的极光B介导的NDC80磷酸化。通过Aurora B激酶的化学​​抑制可以抵押由CENP-E抑制引起的中期染色体未对准。此外，一对单调姐妹 - kinetochores根据CENP-E电机活性显示单极纺锤中的极光介质磷酸化的不对称水平。这些结果共同提出了一种独立于张力的机制，以减少外动脉培养组分的极光介导的磷酸化响应于CENP-E捕获的微管捕获。还2019年，？ 2019年Informa UK Limited，贸易为泰勒和弗朗西斯集团。

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  • 来源
    《Cell cycle》 |2019年第12期|共15页
  • 作者

    Taveras; Liu; C.a; b; Mao; Y.a;

  • 作者单位

    Department of Pathology and Cell Biology Columbia University Vagelos College of Physicians and;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 细胞生物学;
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