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Examination of Mitotic and Meiotic Fission Yeast Nuclear Dynamics by Fluorescence Live-cell Microscopy
Published on: June 24, 2019
The fission yeast MO25 protein functions in polar growth and cell separation
Manuel Mendoza1, Stefanie Redemann, Damian Brunner
1European Molecular Biology Laboratory, Heidelberg, Germany.
Abstract:
Proteins of the MO25 family are widely conserved but their function has not been characterized in detail. Human MO25 is a cofactor of LKB1, a conserved protein kinase with roles in cell polarity in nematodes, flies and mammalian cells. Furthermore, the budding yeast MO25 homologue, Hym1, is important for cell separation and morphogenesis. We have characterized Pmo25p, the MO25 homologue in the fission yeast Schizosaccharomyces pombe. Pmo25p is an essential protein required for polar growth; in its absence the actin cytoskeleton becomes depolarized and cells adopt a round morphology. In addition, pmo25 mutants are defective in cell separation. Both functions of Pmo25p appear to be mediated by the Orb6p-Mob2p kinase complex. Pmo25p shows no distinct localization during interphase, but it is recruited to one of the two spindle pole bodies during anaphase and to the division site during cytokinesis. The septation initiation network (SIN) regulates the localization of Pmo25p, suggesting that it regulates Pmo25p function during cell division.
Insights
The fission yeast protein Pmo25p is essential for cell growth and separation. Its absence disrupts the actin cytoskeleton and cell shape, highlighting its role in cell division regulation.
Area of Science:
- Cell Biology
- Molecular Biology
- Genetics
Background:
- The MO25 protein family is conserved across species, but functional characterization remains limited.
- Human MO25 acts as a cofactor for LKB1, a protein kinase involved in cell polarity.
- Homologues like budding yeast Hym1 are crucial for cell separation and morphogenesis.
Purpose of the Study:
- To characterize the function of Pmo25p, the MO25 homologue in fission yeast (Schizosaccharomyces pombe).
- To investigate the role of Pmo25p in cell polarity, actin cytoskeleton organization, and cell separation.
- To elucidate the regulatory mechanisms and cellular localization of Pmo25p.
Main Methods:
- Genetic analysis of pmo25 deletion mutants in Schizosaccharomyces pombe.
- Microscopic observation of actin cytoskeleton organization and cell morphology.
- Investigation of Pmo25p localization during the cell cycle.
- Analysis of interactions with the Orb6p-Mob2p kinase complex and the septation initiation network (SIN).
Main Results:
- Pmo25p is essential for polar growth; its absence leads to actin cytoskeleton depolarization and a rounded cell morphology.
- pmo25 mutants exhibit defects in cell separation.
- Pmo25p functions via the Orb6p-Mob2p kinase complex.
- Pmo25p localizes to spindle pole bodies during anaphase and the division site during cytokinesis, regulated by the SIN.
Conclusions:
- Pmo25p is a critical regulator of polar growth and cell separation in fission yeast.
- The Orb6p-Mob2p kinase complex mediates Pmo25p's functions in cell division.
- Pmo25p's localization and function are tightly regulated by the septation initiation network during cell division.
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