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

Autor: Seyma Nur Bektas, Hüseyin Karabürk, Cansu Dilege, Ayse Koca Caydasi, Idil Kirdök, Dilara Kocakaplan
Přispěvatelé: Çaydaşı, Ayşe Koca (ORCID 0000-0003-2570-1367 & YÖK ID 252978), Kocakaplan, Dilara, Karabürk, Hüseyin, Dilege, Cansu, Kırdök, İdil, Bektaş, Şeyma Nur, Graduate School of Sciences and Engineering, College of Engineering, Department of Molecular Biology and Genetics
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Saccharomyces cerevisiae Proteins
Cell division
QH301-705.5
Science
Phosphatase
Saccharomyces cerevisiae
S. cerevisiae
Mitosis
Spindle Apparatus
Biology
General Biochemistry
Genetics and Molecular Biology
Spindle pole body
03 medical and health sciences
0302 clinical medicine
Protein Phosphatase 1
signalling
Biology (General)
Life sciences
Biomedicine
Cell cycles
Pindle position checkpoint
PP1
Signalling mitotic exit
S
Cerevisiae
030304 developmental biology
Anaphase
mitotic exit
0303 health sciences
General Immunology and Microbiology
Chemistry
Effector
General Neuroscience
030302 biochemistry & molecular biology
Cell Polarity
Protein phosphatase 1
General Medicine
Cell Biology
Cell cycle
Temperature-sensitive mutant
biology.organism_classification
Spindle apparatus
Cell biology
Mitotic exit
M Phase Cell Cycle Checkpoints
Medicine
cell cycle
030217 neurology & neurosurgery
Research Article
spindle position checkpoint
Zdroj: eLife
bioRxiv
eLife, Vol 10 (2021)
BioRxiv
Popis: 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.
European Molecular Biology Organization (EMBO); Scientific and Technological Research Council of Turkey (TÜBİTAK); European Union (EU); Horizon 2020; European Commission (EC); Department of Biotechnology (DBT) India
Databáze: OpenAIRE
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