期刊论文详细信息
Frontiers in Cell and Developmental Biology
Cell Division Cycle 5-Like Regulates Metaphase-to-Anaphase Transition in Meiotic Oocyte
Jian Li1  Chun-Hui Zhang1  Qing-Yuan Sun2  Tie-Gang Meng2  Hong-Yong Zhang3  Wei-Ping Qian3  Wei Yue4  Ying-Chun Ouyang4 
[1] Department of Reproductive Medicine, Peking University Shenzhen Hospital, Shenzhen Peking University-The Hong Kong University of Science and Technology Medical Center, Shenzhen, China;Fertility Preservation Lab, Reproductive Medicine Center, Guangdong Second Provincial General Hospital, Guangzhou, China;Guangdong Key Laboratory of Male Reproductive Medicine and Genetics, Shenzhen PKU-HKUST Medical Center, Institute of Urology, Peking University Shenzhen Hospital, Shenzhen, China;State Key Laboratory of Stem Cell and Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing, China;
关键词: meiotic progression;    Cdc5L;    securin;    APC/C;    mouse oocyte;   
DOI  :  10.3389/fcell.2021.671685
来源: DOAJ
【 摘 要 】

The quality of oocytes is a vital factor for embryo development. Meiotic progression through metaphase I usually takes a relatively long time to ensure correct chromosome separation, a process that is critical for determining oocyte quality. Here, we report that cell division cycle 5-like (Cdc5L) plays a critical role in regulating metaphase-to-anaphase I transition during mouse oocyte meiotic maturation. Knockdown of Cdc5L by small interfering RNA injection did not affect spindle assembly but caused metaphase I arrest and subsequent reduced first polar body extrusion due to insufficient anaphase-promoting complex/cyclosome activity. We further showed that Cdc5L could also directly interact with securin, and Cdc5L knockdown led to a continuous high expression level of securin, causing severely compromised meiotic progression. The metaphase-to-anaphase I arrest caused by Cdc5L knockdown could be rescued by knockdown of endogenous securin. In summary, we reveal a novel role for Cdc5L in regulating mouse oocyte meiotic progression by interacting with securin.

【 授权许可】

Unknown   

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