Journal
GENES & DEVELOPMENT
Volume 31, Issue 11, Pages 1089-1094Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.302067.117
Keywords
cell division; kinetochore; spindle assembly checkpoint; APC/C; Cdc20; protein phosphatase 1
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Funding
- National Institutes of Health [GM074215]
- Pew Latin American fellowship
- Deutsche Forschungsgemeinschaft [ME 4713/1-1]
- Ludwig Institute for Cancer Research
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Mitotic duration is determined by activation of the anaphase-promoting complex/cyclosome (APC/C) bound to its coactivator, Cdc20. Kinetochores, the microtubuleinteracting machines on chromosomes, restrain mitotic exit when not attached to spindle microtubules by generating a Cdc20-containing complex that inhibits the APC/C. Here, we showthat flux of Cdc20 through kinetochores also accelerates mitotic exit by promoting its dephosphorylation by kinetochore-localized protein phosphatase 1, which allows Cdc20 to activate the APC/C. Both APC/C activation and inhibition depend on Cdc20 fluxing through the same binding site at kinetochores. The microtubule attachment status of kinetochores therefore optimizes mitotic duration by controlling the balance between opposing Cdc20 fates.
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