1. Academic Validation
  2. CENP-F-dependent DRP1 function regulates APC/C activity during oocyte meiosis I

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

  • Nat Commun. 2022 Dec 13;13(1):7732. doi: 10.1038/s41467-022-35461-5.
Cheng-Jie Zhou 1 Xing-Yue Wang 2 Yan-Hua Dong 2 Dong-Hui Wang 2 Zhe Han 2 Xiao-Jie Zhang 2 Qing-Yuan Sun 3 John Carroll 4 Cheng-Guang Liang 5
Affiliations

Affiliations

  • 1 State Key Laboratory of Reproductive Regulation & Breeding of Grassland Livestock, School of Life Sciences, Inner Mongolia University, 010070, Hohhot, Inner Mongolia, China. [email protected].
  • 2 State Key Laboratory of Reproductive Regulation & Breeding of Grassland Livestock, School of Life Sciences, Inner Mongolia University, 010070, Hohhot, Inner Mongolia, China.
  • 3 Fertility Preservation Lab, Guangdong-Hong Kong Metabolism & Reproduction Joint Laboratory, Reproductive Medicine Center, Guangdong Second Provincial General Hospital, 510317, Guangzhou, China.
  • 4 Development and Stem Cells Program, Department of Anatomy and Developmental Biology, Monash Biomedicine Discovery Institute, Monash University, Melbourne, VIC, 3800, Australia.
  • 5 State Key Laboratory of Reproductive Regulation & Breeding of Grassland Livestock, School of Life Sciences, Inner Mongolia University, 010070, Hohhot, Inner Mongolia, China. [email protected].
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.

Figures
Products
  • Cat. No.
    Product Name
    Description
    Target
    Research Area
  • HY-124955
    99.94%, APC Inhibitor
    APC