Protein phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae.
Dilara KocakaplanHüseyin KarabürkCansu DilegeIdil KirdökSeyma Nur BektasAyse Koca CaydasiPublished in: eLife (2021)
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.
Keyphrases
- cell cycle
- dna damage
- saccharomyces cerevisiae
- cell proliferation
- protein protein
- amino acid
- binding protein
- protein kinase
- dendritic cells
- public health
- gene expression
- regulatory t cells
- high resolution
- single cell
- transcription factor
- tyrosine kinase
- small molecule
- bone marrow
- mesenchymal stem cells
- type iii
- genome wide