CLASP1与PRC1的相互作用在中心纺锤体微管构架形成中的功能解析
摘要
细胞分裂时,染色体的分离由纺锤体微管协同动点完成。从纺锤体两极发出的极间微管发生重排,在分开移向两极的染色单体之间形成严密整齐的动态结构:中心纺锤体。中心纺锤体主要由两束稳定的反平行微管构架而成,其担负胞质分裂的启动和完成。参与中心纺锤体形成与维系的重要分子包括有丝分裂马达蛋白(mitotic kinesin),微管捆绑蛋白PRC1以及Aurora B激酶复合物的参与。然而,PRC1在中心纺锤体组成过程中的确切功能及其相关蛋白质群还有待进一步研究。
根据PRC1在中心纺锤体组成过程中的作用,我试图解析PRC1功能蛋白质群的分子构成及其作用机制。我的工作揭示了PRC1与CLASP1相互作用性及其作用域。CLASP1属于一类调节中心纺锤体重叠微管束稳定性的保守蛋白家族。PRC1通过KIF4先于CLASP1驶向中体微管相互作用,并将CLASP1稳定定位到中心纺锤体。下调CLASP1蛋白质的表达会导致姐妹染色单体间染色体桥的产生和中心纺锤体微管发生解聚。为了测试CLASP1-PRC1相互作用对中体微管可塑性的影响,我设计并制备了一个膜通透多肽,竞争性地抑制内源性CLASP1-PRC1蛋白的相互作用。我的活细胞成像实验发现此多肽通过破坏CLASP1-PRC1蛋白的相互作用影响染色体的精确分离,并导致染色体桥的产生。这些发现显示出CLASP1-PRC1相互作用维系中体微管的可塑性及细胞分裂染色体稳定性。为此,我的研究揭示PRC1维系CLASP1在中心纺锤体的定位并通过与CLASP1的作用调控中体微管的可塑性。我认为CLASP1-PRC1复合体负责稳定中心纺锤体微管和维系反平行微管的延伸。
During cell division,chromosome segregation is governed by the interaction of spindle microtubules with the kinetochore.A dramatic remodeling of interpolar microtubules into an organized central spindle between the separating chromatids is required for the initiation and execution of cytokinesis.Central spindle organization requires mitotic kinesins,microtubule-bundling protein PRC1,and Aurora B kinase complex.However,the precise role of PRC1 in central spindle organization has remained elusive.
Here we show that PRC1 recruits CLASP1 to the central spindle at early anaphase onset.CLASP1 belongs to a conserved microtubule-binding protein family that mediates the stabilization of overlapping microtubules of the central spindle. PRC1 physically interacts with CLASP1 and specifies its localization to the central spindle.Repression of CLASP1 leads to sister-chromatid bridges and depolymerization of spindle midzone microtubule.Disruption of CLASP1-PRC1 interaction by a membrane permeable peptide abrogates accurate chromosome segregation,resulting in sister chromatid bridges.These findings reveal a key role for the CLASP1-PRC1 interaction in achieving a stable anti-parallel microtubule organization essential for faithful chromosome segregation.We propose that PRC1 forms a link between stabilization of CLASP1 association with central spindle microtubules and anti-parallel microtubule elongation.
根据PRC1在中心纺锤体组成过程中的作用,我试图解析PRC1功能蛋白质群的分子构成及其作用机制。我的工作揭示了PRC1与CLASP1相互作用性及其作用域。CLASP1属于一类调节中心纺锤体重叠微管束稳定性的保守蛋白家族。PRC1通过KIF4先于CLASP1驶向中体微管相互作用,并将CLASP1稳定定位到中心纺锤体。下调CLASP1蛋白质的表达会导致姐妹染色单体间染色体桥的产生和中心纺锤体微管发生解聚。为了测试CLASP1-PRC1相互作用对中体微管可塑性的影响,我设计并制备了一个膜通透多肽,竞争性地抑制内源性CLASP1-PRC1蛋白的相互作用。我的活细胞成像实验发现此多肽通过破坏CLASP1-PRC1蛋白的相互作用影响染色体的精确分离,并导致染色体桥的产生。这些发现显示出CLASP1-PRC1相互作用维系中体微管的可塑性及细胞分裂染色体稳定性。为此,我的研究揭示PRC1维系CLASP1在中心纺锤体的定位并通过与CLASP1的作用调控中体微管的可塑性。我认为CLASP1-PRC1复合体负责稳定中心纺锤体微管和维系反平行微管的延伸。
During cell division,chromosome segregation is governed by the interaction of spindle microtubules with the kinetochore.A dramatic remodeling of interpolar microtubules into an organized central spindle between the separating chromatids is required for the initiation and execution of cytokinesis.Central spindle organization requires mitotic kinesins,microtubule-bundling protein PRC1,and Aurora B kinase complex.However,the precise role of PRC1 in central spindle organization has remained elusive.
Here we show that PRC1 recruits CLASP1 to the central spindle at early anaphase onset.CLASP1 belongs to a conserved microtubule-binding protein family that mediates the stabilization of overlapping microtubules of the central spindle. PRC1 physically interacts with CLASP1 and specifies its localization to the central spindle.Repression of CLASP1 leads to sister-chromatid bridges and depolymerization of spindle midzone microtubule.Disruption of CLASP1-PRC1 interaction by a membrane permeable peptide abrogates accurate chromosome segregation,resulting in sister chromatid bridges.These findings reveal a key role for the CLASP1-PRC1 interaction in achieving a stable anti-parallel microtubule organization essential for faithful chromosome segregation.We propose that PRC1 forms a link between stabilization of CLASP1 association with central spindle microtubules and anti-parallel microtubule elongation.
引文
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