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Updated: Jun 14, 2025

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast
Published on: February 20, 2017
Roles of the MO25 protein Pmo25 in contractile-ring stability and localization of the NDR kinase Sid2 during
Yanfang Ye1,2, Sha Zhang1, Aysha H Osmani1,3
1Department of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA.
Abstract:
Mouse protein-25 (MO25) family proteins are crucial in development and morphogenesis from plants to humans. The fission yeast MO25 protein Pmo25 is essential for cell polarity and division. However, how Pmo25 regulates cytokinesis remains largely unknown. Here we found that the actomyosin contractile ring and septum formation were defective during cytokinesis in pmo25 mutants. Pmo25 physically and genetically interacted with the myosin-II light chain Cdc4, which is essential for the contractile-ring assembly and function. Additionally, pmo25 mutations had synthetic genetic interactions with all other tested mutations in contractile-ring proteins. Moreover, Pmo25 colocalized with the NDR kinase Sid2 and participated in its recruitment to the division plane. Furthermore, Pmo25 directly bound the Munc13/UNC-13 protein Ync13 and modulated the secretion of glucanase Eng1 to the division site for daughter-cell separation. Our data provide insight into how Pmo25 regulates cytokinesis and suggest that the conserved MO25 proteins can link various steps of cytokinesis.
Insights
Mouse protein-25 (MO25) is vital for cell division. This study shows MO25 protein Pmo25 interacts with key proteins to ensure stable contractile rings and proper cell separation in fission yeast.
Area of Science:
- Cell Biology
- Molecular Biology
- Genetics
Background:
- Mouse protein-25 (MO25) proteins are essential for development and morphogenesis across diverse organisms.
- In fission yeast, Pmo25 is critical for maintaining cell polarity and division.
- The precise role of Pmo25 in regulating cytokinesis is not well understood.
Purpose of the Study:
- To elucidate the molecular mechanism by which Pmo25 regulates cytokinesis in fission yeast.
- To identify proteins that interact with Pmo25 and contribute to its function in cell division.
Main Methods:
- Yeast two-hybrid screening to identify interacting proteins.
- Co-immunoprecipitation and in-vitro binding assays to confirm interactions.
- Analysis of cytokinesis defects in pmo25 mutant strains.
Main Results:
- Pmo25 directly binds to Ync13, a Munc13/UNC-13 family protein.
- pmo25 mutants exhibit defective contractile-ring stability and septation, with rings sliding or disintegrating.
- Pmo25 interacts with Cdc4, the myosin-II light chain, crucial for contractile-ring assembly.
- Division-site recruitment of Sid2 kinase and Eng1 glucanase is impaired in pmo25 mutants.
Conclusions:
- Pmo25 plays a novel role in regulating cytokinesis by stabilizing the contractile ring and ensuring proper recruitment of key division proteins.
- The findings reveal a conserved mechanism for MO25 proteins in linking various cellular processes, including cell division.
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