MASTL promotes cyclin B1 destruction by enforcing Cdc20-independent binding of cyclin B1 to the APC/C

Biology Open
Erik Voets, Rob Wolthuis

Abstract

When cells enter mitosis, the anaphase-promoting complex/cyclosome (APC/C) is activated by phosphorylation and binding of Cdc20. The RXXL destruction box (D-box) of cyclin B1 only binds Cdc20 after release of the spindle checkpoint in metaphase, initiating cyclin B1 ubiquitination upon chromosome bi-orientation. However, we found that cyclin B1, through Cdk1 and Cks, is targeted to the phosphorylated APC/C(Cdc20) at the start of prometaphase, when the spindle checkpoint is still active. Here, we show that MASTL is essential for cyclin B1 recruitment to the mitotic APC/C and that this occurs entirely independently of Cdc20. Importantly, MASTL-directed binding of cyclin B1 to spindle checkpoint-inhibited APC/C(Cdc20) critically supports efficient cyclin B1 destruction after checkpoint release. A high incidence of anaphase bridges observed in response to MASTL RNAi may result from cyclin B1 remaining after securin destruction, which is insufficient to keep MASTL-depleted cells in mitosis but delays the activation of separase.

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Citations

Oct 19, 2017·Cancer Metastasis Reviews·Dong WangWenyi Wei
Dec 18, 2018·Frontiers in Cell and Developmental Biology·Kamila Marzec, Andrew Burgess
Oct 26, 2018·Journal of Cell Science·Anna Castro, Thierry Lorca
Jun 14, 2017·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·Jianjun TianJianhua Yu

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Methods Mentioned

BETA
transfection
transfections
immunoprecipitation
pull-down
immunoprecipitations
pulls down
biosensor
pull down

Software Mentioned

MASTL
ImageJ
Illustrator
Adobe
Photoshop

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