Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae

eLife

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