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The Borealin dimerization domain interacts with Sgo1 to drive Aurora B-mediated spindle assembly.
Molecular Biology of the Cell ( IF 3.3 ) Pub Date : 2020-07-22 , DOI: 10.1091/mbc.e20-05-0341
Mary Kate Bonner 1 , Julian Haase 1 , Hayden Saunders 1 , Hindol Gupta 1 , Biyun Iris Li 1 , Alexander E Kelly 1
Affiliation  

The Chromosomal Passenger Complex (CPC), which includes the kinase Aurora B, is a master regulator of meiotic and mitotic processes that ensure the equal segregation of chromosomes. Sgo1 is thought to play a major role in the recruitment of the CPC to chromosomes, but the molecular mechanism and contribution of Sgo1-dependent CPC recruitment is currently unclear. Using Xenopus egg extracts and biochemical reconstitution, we found that Sgo1 directly interacts with the dimerization domain of the CPC subunit Borealin. Borealin and the PP2A phosphatase complex can simultaneously bind to the coiled coil domain of Sgo1, suggesting that Sgo1 can integrate Aurora B and PP2A activities to modulate Aurora B substrate phosphorylation. A Borealin mutant that specifically disrupts the Sgo1-Borealin interaction results in defects in CPC chromosomal recruitment and Aurora B-dependent spindle assembly, but not in spindle assembly checkpoint (SAC) signaling at unattached kinetochores. These findings establish a direct molecular connection between Sgo1 and the CPC, and have major implications for the different functions of Aurora B that promote the proper interaction between spindle microtubules and chromosomes.



中文翻译:

Borealin二聚结构域与Sgo1相互作用以驱动Aurora B介导的纺锤体组装。

包括激酶Aurora B的染色体乘客复合体(CPC)是减数分裂和有丝分裂过程的主要调节剂,可确保染色体的平等分离。Sgo1被认为在CPC的染色体募集中起主要作用,但是目前尚不清楚Sgo1依赖的CPC募集的分子机制和贡献。使用非洲爪蟾卵提取物和生化重构,我们发现Sgo1与CPC亚基Borealin的二聚化域直接相互作用。Borealin和PP2A磷酸酶复合物可以同时结合到Sgo1的卷曲螺旋结构域,这表明Sgo1可以整合Aurora B和PP2A活性来调节Aurora B底物的磷酸化。特异性破坏Sgo1-Borealin相互作用的Borealin突变体会导致CPC染色体募集和Aurora B依赖的纺锤体组装中的缺陷,但不会导致未连接的动植物的纺锤体组装检查点(SAC)信号产生缺陷。这些发现建立了Sgo1和CPC之间的直接分子联系,并对Aurora B的不同功能具有重要意义,这些功能可促进纺锤体微管和染色体之间的正确相互作用。

更新日期:2020-08-20
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