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Cdk1 negatively regulates the spindle localization of Prc1 in mouse oocytes
Author(s) -
Nishiyama Sui,
Yoshida Shuhei,
Kitajima Tomoya S.
Publication year - 2020
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/gtc.12803
Subject(s) - microbiology and biotechnology , biology , meiosis , spindle checkpoint , kinetochore , cyclin dependent kinase 1 , spindle pole body , multipolar spindles , spindle apparatus , chromosome segregation , oocyte , genetics , cell cycle , embryo , cell division , chromosome , cell , gene
Chromosome segregation requires the formation of a bipolar spindle. The timely bipolarization of the acentrosomal spindle during meiosis I in mouse oocytes depends on the antiparallel microtubule crosslinker Prc1. How Prc1 is regulated in oocytes remains poorly understood. In this study, we show that the kinase Cdk1 negatively regulates the spindle localization of Prc1 in mouse oocytes. The acute inhibition of Cdk1 activity led to excessive localization of Prc1 at the spindle and kinetochores, whereas the overactivation of Cdk1 had opposite effects. The overexpression of Prc1 carrying mutations at Cdk1‐mediated phosphorylation sites increased its localization to the spindle, accelerated spindle bipolarization and caused spindle‐checkpoint‐dependent arrest at metaphase I. Overactivation of Cdk1 delayed spindle bipolarization, which was reversed by the overexpression of a phospho‐mutant form but not the wild‐type form of Prc1. These results suggest that Cdk1‐mediated phosphorylation negatively regulates Prc1 localization to ensure the timely bipolarization of the acentrosomal spindle during meiosis I in mammalian oocytes.