CENP-F-dependent DRP1 function regulates APC/C activity during oocyte meiosis I

Cheng-Jie Zhou (), Xing-Yue Wang, Yan-Hua Dong, Dong-Hui Wang, Zhe Han, Xiao-Jie Zhang, Qing-Yuan Sun, John Carroll and Cheng-Guang Liang ()
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Cheng-Jie Zhou: Inner Mongolia University
Xing-Yue Wang: Inner Mongolia University
Yan-Hua Dong: Inner Mongolia University
Dong-Hui Wang: Inner Mongolia University
Zhe Han: Inner Mongolia University
Xiao-Jie Zhang: Inner Mongolia University
Qing-Yuan Sun: Guangdong Second Provincial General Hospital
John Carroll: Monash University
Cheng-Guang Liang: Inner Mongolia University

Nature Communications, 2022, vol. 13, issue 1, 1-17

Abstract: Abstract Chromosome segregation is initiated by cohesin degradation, which is driven by anaphase-promoting complex/cyclosome (APC/C). Chromosome cohesin is removed by activated separase, with the degradation of securin and cyclinB1. Dynamin-related protein 1 (DRP1), a component of the mitochondrial fission machinery, is related to cyclin dynamics in mitosis progression. Here, we show that DRP1 is recruited to the kinetochore by centromeric Centromere protein F (CENP-F) after nuclear envelope breakdown in mouse oocytes. Loss of DRP1 during prometaphase leads to premature cohesin degradation and chromosome segregation. Importantly, acute DRP1 depletion activates separase by initiating cyclinB1 and securin degradation during the metaphase-to-anaphase transition. Finally, we demonstrate that DRP1 is bound to APC2 to restrain the E3 ligase activity of APC/C. In conclusion, DRP1 is a CENP-F-dependent atypical spindle assembly checkpoint (SAC) protein that modulates metaphase-to-anaphase transition by controlling APC/C activity during meiosis I in oocytes.

Date: 2022
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DOI: 10.1038/s41467-022-35461-5

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