TY - JOUR T1 - Protein Phosphatase 1 in association with Bud14 inhibits mitotic exit in <em>Saccharomyces cerevisiae</em> JF - bioRxiv DO - 10.1101/2020.08.30.273946 SP - 2020.08.30.273946 AU - Dilara Kocakaplan AU - Hüseyin Karabürk AU - Cansu Dilege AU - Idil Kirdok AU - Şeyma Nur Bektaş AU - Ayse Koca Caydasi Y1 - 2021/01/01 UR - http://biorxiv.org/content/early/2021/08/05/2020.08.30.273946.abstract N2 - 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.Competing Interest StatementThe authors have declared no competing interest. ER -