eLife | |
Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae | |
Ayse Koca Caydasi1  Dilara Kocakaplan1  Seyma Nur Bektas1  Hüseyin Karabürk1  Idil Kirdök1  Cansu Dilege1  | |
[1] Department of Molecular Biology and Genetics, Koç University, Istanbul, Turkey; | |
关键词: cell cycle; spindle position checkpoint; PP1; signalling; mitotic exit; S. cerevisiae; | |
DOI : 10.7554/eLife.72833 | |
来源: eLife Sciences Publications, Ltd | |
【 摘 要 】
Mitotic exit in budding yeast is dependent on correct orientation of the mitotic spindle along the cell polarity axis. When accurate positioning of the spindle fails, a surveillance mechanism named the spindle position checkpoint (SPOC) prevents cells from exiting mitosis. Mutants with a defective SPOC become multinucleated and lose their genomic integrity. Yet, a comprehensive understanding of the SPOC mechanism is missing. In this study, we identified the type 1 protein phosphatase, Glc7, in association with its regulatory protein Bud14 as a novel checkpoint component. We further showed that Glc7-Bud14 promotes dephosphorylation of the SPOC effector protein Bfa1. Our results suggest a model in which two mechanisms act in parallel for a robust checkpoint response: first, the SPOC kinase Kin4 isolates Bfa1 away from the inhibitory kinase Cdc5, and second, Glc7-Bud14 dephosphorylates Bfa1 to fully activate the checkpoint effector.
【 授权许可】
CC BY
【 预 览 】
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RO202112118858446ZK.pdf | 3509KB | download |