IF 11.7 1区 综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES
Yu Zhang, Jie Bai, Bo Xiong
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引用次数: 0

摘要

在有丝分裂过程中,染色体的准确分离和基因组的稳定需要由凝聚素复合体及其相关蛋白介导的染色体内聚力。然而,由于运行机制不同,许多蛋白在生殖细胞减数分裂过程中可能发挥不同的功能。在这里,我们记录了凝聚素相关蛋白姐妹早熟解离5A(Pds5A)在卵母细胞成熟过程中的减数分裂纺锤体组装过程中发挥的非规范作用,而与其凝聚功能无关。Pds5A 在卵母细胞的移行期 I 和移行期 II 阶段都分布在纺锤体纤维上。基于phospholino的Pds5A耗竭或基因消减都会导致卵母细胞中纺锤体组织、染色体整倍体和减数分裂进程的缺陷,从而影响女性的生育能力。从机理上讲,Pds5A 将去泛素化酶泛素特异性蛋白酶 14 招募到纺锤体上,以稳定驱动蛋白家族成员 5B,从而调节纺锤体的伸长。总之,我们的研究结果揭示了凝聚素相关蛋白Pds5A在卵母细胞减数分裂过程中可作为纺锤体调节器。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

The cohesin-associated protein Pds5A governs the meiotic spindle assembly via deubiquitination of Kif5B in oocytes

The cohesin-associated protein Pds5A governs the meiotic spindle assembly via deubiquitination of Kif5B in oocytes
Chromosome cohesion mediated by cohesin complex and its associated proteins is required for accurate chromosome segregation and genomic stability in mitosis. However, because of the distinct operation mechanisms, many proteins might exert different functions during meiosis in germ cells. Here, we document that cohesin-associated protein precocious dissociation of sisters 5A (Pds5A) plays a noncanonical role in the meiotic spindle assembly during oocyte maturation independent of its cohesion function. Pds5A distributes on the spindle fibers in oocytes at both metaphase I and metaphase II stages. Morpholino-based depletion or genetic ablation of Pds5A all lead to defects in spindle organization, chromosome euploidy and meiotic progression in oocytes and thus compromising the female fertility. Mechanistically, Pds5A recruits deubiquitinase ubiquitin-specific protease 14 to the spindle apparatus for stabilization of kinesin family member 5B, regulating the spindle elongation. Collectively, our findings unveil that cohesin-associated protein Pds5A can be used as a spindle regulator during oocyte meiosis.
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来源期刊
Science Advances
Science Advances 综合性期刊-综合性期刊
CiteScore
21.40
自引率
1.50%
发文量
1937
审稿时长
29 weeks
期刊介绍: Science Advances, an open-access journal by AAAS, publishes impactful research in diverse scientific areas. It aims for fair, fast, and expert peer review, providing freely accessible research to readers. Led by distinguished scientists, the journal supports AAAS's mission by extending Science magazine's capacity to identify and promote significant advances. Evolving digital publishing technologies play a crucial role in advancing AAAS's global mission for science communication and benefitting humankind.
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