Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae
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 S...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications Ltd
2021-10-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/72833 |
| _version_ | 1811227718526697472 |
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| author | Dilara Kocakaplan Hüseyin Karabürk Cansu Dilege Idil Kirdök Seyma Nur Bektas Ayse Koca Caydasi |
| author_facet | Dilara Kocakaplan Hüseyin Karabürk Cansu Dilege Idil Kirdök Seyma Nur Bektas Ayse Koca Caydasi |
| author_sort | Dilara Kocakaplan |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T09:46:26Z |
| format | Article |
| id | doaj.art-3b21a37de7764c95a7c54554b4c3589a |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T09:46:26Z |
| publishDate | 2021-10-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-3b21a37de7764c95a7c54554b4c3589a2022-12-22T03:37:56ZengeLife Sciences Publications LtdeLife2050-084X2021-10-011010.7554/eLife.72833Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiaeDilara Kocakaplan0Hüseyin Karabürk1Cansu Dilege2Idil Kirdök3Seyma Nur Bektas4Ayse Koca Caydasi5https://orcid.org/0000-0003-2570-1367Department of Molecular Biology and Genetics, Koç University, Istanbul, TurkeyDepartment of Molecular Biology and Genetics, Koç University, Istanbul, TurkeyDepartment of Molecular Biology and Genetics, Koç University, Istanbul, TurkeyDepartment of Molecular Biology and Genetics, Koç University, Istanbul, TurkeyDepartment of Molecular Biology and Genetics, Koç University, Istanbul, TurkeyDepartment of Molecular Biology and Genetics, Koç University, Istanbul, TurkeyMitotic 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.https://elifesciences.org/articles/72833cell cyclespindle position checkpointPP1signallingmitotic exit |
| spellingShingle | Dilara Kocakaplan Hüseyin Karabürk Cansu Dilege Idil Kirdök Seyma Nur Bektas Ayse Koca Caydasi Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae eLife cell cycle spindle position checkpoint PP1 signalling mitotic exit |
| title | Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae |
| title_full | Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae |
| title_fullStr | Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae |
| title_full_unstemmed | Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae |
| title_short | Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae |
| title_sort | protein phosphatase 1 in association with bud14 inhibits mitotic exit in saccharomyces cerevisiae |
| topic | cell cycle spindle position checkpoint PP1 signalling mitotic exit |
| url | https://elifesciences.org/articles/72833 |
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