Separase cleaves the kinetochore protein Meikin at the meiosis I/II transition
Name
nihms-1721767.pdf
Description
Accepted version
Size
3.33 MB
Format
Adobe PDF
Checksum (MD5)
eac4952051970cc8dda61e8ade30cb66
Author(s)
Maier, Nolan K
Ma, Jun
Lampson, Michael A
Cheeseman, Iain M
Date Issued
2021
Journal
Developmental Cell
Publisher
Elsevier BV
Citation
Maier, Nolan K, Ma, Jun, Lampson, Michael A and Cheeseman, Iain M. 2021. "Separase cleaves the kinetochore protein Meikin at the meiosis I/II transition." Developmental Cell, 56 (15).
Version
Author's final manuscript
Abstract
To generate haploid gametes, germ cells undergo two consecutive meiotic divisions requiring key changes to the cell division machinery. Here, we demonstrate that the protease separase rewires key cell division processes at the meiosis I/II transition by cleaving the meiosis-specific protein Meikin. Separase proteolysis does not inactivate Meikin but instead alters its function to create a distinct activity state. Full-length Meikin and the C-terminal Meikin separase cleavage product both localize to kinetochores, bind to Plk1 kinase, and promote Rec8 cleavage, but our results reveal distinct roles for these proteins in controlling meiosis. Mutations that prevent Meikin cleavage or that conditionally inactivate Meikin at anaphase I result in defective meiosis II chromosome alignment in mouse oocytes. Finally, as oocytes exit meiosis, C-Meikin is eliminated by APC/C-mediated degradation prior to the first mitotic division. Thus, multiple regulatory events irreversibly modulate Meikin activity during successive meiotic divisions to rewire the cell division machinery at two distinct transitions.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Terms of Use
Creative Commons Attribution-NonCommercial-NoDerivs License
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DOI of Published Version
https://doi.org/10.1016/J.DEVCEL.2021.06.019
