Cyclin B1-Cdk1 facilitates MAD1 release from the nuclear pore to ensure a robust spindle checkpoint.
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Date
2020-06-01Author
Jackman, M
Marcozzi, C
Barbiero, M
Pardo, M
Yu, L
Tyson, AL
Choudhary, JS
Pines, J
Type
Journal Article
Metadata
Show full item recordAbstract
How the cell rapidly and completely reorganizes its architecture when it divides is a problem that has fascinated researchers for almost 150 yr. We now know that the core regulatory machinery is highly conserved in eukaryotes, but how these multiple protein kinases, protein phosphatases, and ubiquitin ligases are coordinated in space and time to remodel the cell in a matter of minutes remains a major question. Cyclin B1-Cdk is the primary kinase that drives mitotic remodeling; here we show that it is targeted to the nuclear pore complex (NPC) by binding an acidic face of the kinetochore checkpoint protein, MAD1, where it coordinates NPC disassembly with kinetochore assembly. Localized cyclin B1-Cdk1 is needed for the proper release of MAD1 from the embrace of TPR at the nuclear pore so that it can be recruited to kinetochores before nuclear envelope breakdown to maintain genomic stability.
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Research team
Functional Proteomics Group
Language
eng
Date accepted
2020-03-06
License start date
2020-06
Citation
The Journal of cell biology, 2020, 219 (6)
Publisher
ROCKEFELLER UNIV PRESS