Plk1 negatively regulates Cep55 recruitment to the midbody to ensure orderly abscission.
Plk1 negatively regulates Cep55 recruitment to the midbody to ensure orderly abscission.
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DOI：
10.1083/jcb.201008108
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发表时间：
2010-11-15
期刊：
影响因子：
--
通讯作者：
Barr FA
中科院分区：
文献类型：
--
作者：
Bastos RN;Barr FA
Plk1在有丝分裂退出过程中的降解允许Cep55解离因子的募集和及时的胞质分裂。胞质分裂需要在染色体分离、卵裂沟形成和收缩完成后发生的称为分裂的膜重塑和分裂事件。在这项研究中，我们展示了如何通过Polo样激酶1（Plk1）控制的转录因子的招募。在中期后期过渡，Plk1启动卵裂沟的形成，然后在有丝分裂退出过程中逐步降解。在此期间，Plk1磷酸化的转录因子Cep55的反式，并防止其不合时宜的招聘后期纺锤体。Cep55的Plk1磷酸化位点突变体过早地被募集到后期纺锤体，并且不能支持分裂。内源性Cep55在药物BI 2536或GW 842862抑制Plk1后表现相似。只有Plk1被降解，Cep55才能靶向中间体并促进降解。阻断Plk1降解导致中段Plk1水平升高和Cep55募集失败。因此，Plk1活性负调控Cep55，以确保有序的收缩因子募集，并确保这只发生在细胞收缩完成后。
Degradation of Plk1 during mitotic exit allows recruitment of the Cep55 abscission factor and timely cytokinesis. Cytokinesis requires a membrane-remodeling and fission event termed abscission that occurs after chromosome segregation, cleavage furrow formation, and contraction have completed. In this study, we show how abscission factor recruitment is controlled by the Polo-like kinase 1 (Plk1). At the metaphase–anaphase transition, Plk1 initiates cleavage furrow formation and is then progressively degraded during mitotic exit. During this period, Plk1 phosphorylates the abscission factor Cep55 in trans and prevents its untimely recruitment to the anaphase spindle. A Plk1 phosphorylation site mutant of Cep55 is prematurely recruited to the anaphase spindle and fails to support abscission. Endogenous Cep55 behaves similarly after Plk1 inhibition by the drugs BI2536 or GW842862. Only once Plk1 is degraded can Cep55 target to the midbody and promote abscission. Blocking Plk1 degradation leads to elevated levels of Plk1 at the midbody and the failure of Cep55 recruitment. Thus, Plk1 activity negatively regulates Cep55 to ensure orderly abscission factor recruitment and ensures that this occurs only once cell contraction has completed.
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DOI：
10.1083/jcb.129.6.1617
发表时间：
1995-06
期刊：
The Journal of cell biology
影响因子：
--
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DOI：
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