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Centlein mediates an interaction between C-Nap1 and Cep68 to maintain centrosome cohesion

机译:Centlein介导C-Nap1和Cep68之间的相互作用,以维持中心体凝聚力

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Centrosome cohesion, mostly regarded as a proteinaceous linker between parental centrioles, ensures that the interphase centrosome(s) function as a single microtubule-organizing center. Impairment of centrosome cohesion leads to the splitting of centrosomes. Although the list of cohesion proteins is growing, the precise composition and regulation of centrosome cohesion are still largely unknown. In this study, we show that the centriolar protein centlein (also known as CNTLN) localizes to the proximal ends of the centrioles and directly interacts with both C-Nap1 (also known as Cep250) and Cep68. Moreover, centlein complexes with C-Nap1 and Cep68 at the proximal ends of centrioles during interphase and functions as a molecular link between C-Nap1 and Cep68. Depletion of centlein impairs recruitment of Cep68 to the centrosomes and, in turn, results in centrosome splitting. Both centlein and Cep68 are novel Nek2A substrates. Collectively, our data demonstrate that centrosome cohesion is maintained by the newly identified complex of C-Nap1-centlein-Cep68.
机译:中心体凝聚力,通常被视为亲代中心体之间的蛋白质连接体,可确保相间中心体作为单个微管组织中心发挥作用。中心体凝聚力的损害导致中心体分裂。尽管内聚蛋白的列表在增长,但中心体内聚的精确组成和调控仍是未知之数。在这项研究中,我们显示中心粒蛋白中心蛋白(也称为CNTLN)位于中心粒的近端,并且直接与C-Nap1(也称为Cep250)和Cep68相互作用。此外,在中间相期间,在中心粒的近端处,蛋白素与C-Nap1和Cep68形成复合物,并充当C-Nap1和Cep68之间的分子连接。中心蛋白的耗竭会削弱Cep68向中心体的募集,进而导致中心体分裂。 centlein和Cep68均为新型Nek2A底物。总体而言,我们的数据表明,新确定的C-Nap1-centlein-Cep68复合物可维持中心体凝聚力。

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