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Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Mitotic Exit Function of Polo-like Kinase Cdc5 Is Dependent on Sequential Activation by Cdk1
Jose-Antonio Rodriguez-Rodriguez1, Yolanda Moyano1, Soraya Játiva1
1Cell Cycle Group, Cancer Epigenetics and Biology Program (PEBC), Bellvitge Biomedical Research Institute (IDIBELL), Avenida Gran Via de L'Hospitalet 199-203, 08908 L'Hospitalet de Llobregat, Barcelona, Spain.
The study reveals how Cdc5 polo-like kinase, activated by Cdk1, works independently of the MEN pathway to ensure timely Cdc14 release for mitotic exit in Saccharomyces cerevisiae.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Mitotic exit in Saccharomyces cerevisiae requires Cdc14 activation.
- Two pathways, FEAR and MEN, regulate Cdc14.
- The precise role of Cdc5 polo-like kinase in Cdc14 release is unclear.
Purpose of the Study:
- To elucidate the mechanism by which Cdc5 contributes to timely Cdc14 release.
- To investigate the specific role of Cdc5 in mitotic exit regulation.
Main Methods:
- Genetic analysis
- Biochemical assays
- Phosphorylation studies
Main Results:
- Cdc5 functions in parallel with the MEN pathway during anaphase.
- Cdc5's MEN-independent function requires active separase.
- Cdk1-dependent phosphorylation activates Cdc5 in early anaphase and promotes its MEN-related functions in late anaphase.
Conclusions:
- Cdc5 is a key regulator of Cdc14 release, acting both independently and in conjunction with the MEN pathway.
- Cdk1-mediated phosphorylation is crucial for Cdc5 activation and function in mitotic exit.
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