Aurora B对Bacp/Nlp的磷酸化调控及其参与胞质分裂的机制研究
摘要
胞质分裂是细胞有丝分裂的最后完成阶段,是将倍增的细胞内容物分配到两个独立的子代细胞的最后步骤。胞质分裂是一个有许多因子共同参与的复杂过程,胞质分裂异常,可以导致细胞的染色体不稳定性和细胞癌变等恶性表型。
Bacp/Nlp (BRCA1相关中心体蛋白/Ninein样蛋白)是我室通过酵母双杂交实验自行定位克隆的与BRCA1相关的蛋白,多项研究结果表明,Bacp/Nlp在细胞的有丝分裂过程中参与微管的生发以及纺锤体的形成等重要过程。
在本课题的研究中,我们发现Bacp/Nlp也参与了胞质分裂的过程,当抑制细胞中Bacp/Nlp的表达时,细胞的胞质分裂过程被干扰进而导致细胞多核现象的发生。本研究发现,Bacp/Nlp在胞质分裂过程中的功能发挥依赖其与Aurora B(一种在胞质分裂过程中起重要作用的激酶)的相互作用,干扰它们的相互作用,胞质分裂不能正常进行。通过一系列的体外激酶实验,我们发现Bacp/Nlp是Aurora B的磷酸化底物,其磷酸化反应主要发生在Ser185、Ser448和Ser585三个保守位点。AuroraB对Bacp/Nlp的磷酸化具有两个方面的调控意义：(1)Ser448和Ser585位点的磷酸化对Bacp/Nlp具有募集作用,是Bacp/Nlp在胞质分裂期定位于中间体的前提；
(2)Ser185位点的磷酸化能够稳定Bacp/Nlp,抑制其泛素化降解。
综上所述,本文研究了Aurora B对Bacp/Nlp的磷酸化调控作用,并探讨其对胞质分裂的影响,为深入阐明胞质分裂的调控机制以及认识胞质分裂异常导致基因组不稳定性提供理论基础。
Cytokinesis is the final but critical step of cell division by which the daughter cells are separated completely. Cytokinesis is such a complex process in which many molecules are involved. The aberrant process of cytokinesis could lead to malignant phenotype of cells.
Bacp/Nlp (BRCA1 associated centrosomal protein/Ninein like protein) is a recently identified centrosomal protein which was found by our laboratory through yeast two hybrid approach using the C-terminal of BRCA1. It has been demonstrated to involve in the process of mitosis, including microtubule nucleation and spindle formation.
In this study, we have found that Bacp/Nlp also contributes to regulation of cytokinesis. RNAi-mediated depletion of Bacp/Nlp could perturb the process of cytokinesis and then led to multinucleation. The modality of Bacp/Nlp involving in cytokinesis depends on its interaction with Aurora B in the final stage of mitosis. Inhibition of their interaction could lead to the failure of cytokinesis. Furthermore, we have identified Bacp/Nlp as the substrate of Aurora B. Phosphorylation of Bacp/Nlp by Aurora B acts in the final stage of cell division and affects the completion of cytokinesis. In addition, we mapped the special phsophorylating sites (Serl85, Ser448 and Ser585) of Bacp/Nlp, which have two different functions:first, phosphorylation on Ser448 and Ser585 is necessary for the localization of Bacp/Nlp in midbody; second, phosphorylation on Serl85 could stabilize Bacp/Nlp protein.
Taken together, this study has explored one of the mechanisms for the role of Bacp/Nlp in the control of mitotic progression and demonstrated Aurora B regulation of Bacp/Nlp in the process of cytokinesis, providing novel insights into understanding on the process of cytokinesis.
Bacp/Nlp (BRCA1相关中心体蛋白/Ninein样蛋白)是我室通过酵母双杂交实验自行定位克隆的与BRCA1相关的蛋白,多项研究结果表明,Bacp/Nlp在细胞的有丝分裂过程中参与微管的生发以及纺锤体的形成等重要过程。
在本课题的研究中,我们发现Bacp/Nlp也参与了胞质分裂的过程,当抑制细胞中Bacp/Nlp的表达时,细胞的胞质分裂过程被干扰进而导致细胞多核现象的发生。本研究发现,Bacp/Nlp在胞质分裂过程中的功能发挥依赖其与Aurora B(一种在胞质分裂过程中起重要作用的激酶)的相互作用,干扰它们的相互作用,胞质分裂不能正常进行。通过一系列的体外激酶实验,我们发现Bacp/Nlp是Aurora B的磷酸化底物,其磷酸化反应主要发生在Ser185、Ser448和Ser585三个保守位点。AuroraB对Bacp/Nlp的磷酸化具有两个方面的调控意义：(1)Ser448和Ser585位点的磷酸化对Bacp/Nlp具有募集作用,是Bacp/Nlp在胞质分裂期定位于中间体的前提；
(2)Ser185位点的磷酸化能够稳定Bacp/Nlp,抑制其泛素化降解。
综上所述,本文研究了Aurora B对Bacp/Nlp的磷酸化调控作用,并探讨其对胞质分裂的影响,为深入阐明胞质分裂的调控机制以及认识胞质分裂异常导致基因组不稳定性提供理论基础。
Cytokinesis is the final but critical step of cell division by which the daughter cells are separated completely. Cytokinesis is such a complex process in which many molecules are involved. The aberrant process of cytokinesis could lead to malignant phenotype of cells.
Bacp/Nlp (BRCA1 associated centrosomal protein/Ninein like protein) is a recently identified centrosomal protein which was found by our laboratory through yeast two hybrid approach using the C-terminal of BRCA1. It has been demonstrated to involve in the process of mitosis, including microtubule nucleation and spindle formation.
In this study, we have found that Bacp/Nlp also contributes to regulation of cytokinesis. RNAi-mediated depletion of Bacp/Nlp could perturb the process of cytokinesis and then led to multinucleation. The modality of Bacp/Nlp involving in cytokinesis depends on its interaction with Aurora B in the final stage of mitosis. Inhibition of their interaction could lead to the failure of cytokinesis. Furthermore, we have identified Bacp/Nlp as the substrate of Aurora B. Phosphorylation of Bacp/Nlp by Aurora B acts in the final stage of cell division and affects the completion of cytokinesis. In addition, we mapped the special phsophorylating sites (Serl85, Ser448 and Ser585) of Bacp/Nlp, which have two different functions:first, phosphorylation on Ser448 and Ser585 is necessary for the localization of Bacp/Nlp in midbody; second, phosphorylation on Serl85 could stabilize Bacp/Nlp protein.
Taken together, this study has explored one of the mechanisms for the role of Bacp/Nlp in the control of mitotic progression and demonstrated Aurora B regulation of Bacp/Nlp in the process of cytokinesis, providing novel insights into understanding on the process of cytokinesis.
引文
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