Regulation of Cell Cycle and Shape by Polarity Proteins and Mitotic Exit Network in Yeast

Overview

Cell cycle regulation is essential for both cell health and cancer prevention. Saccharomyces cerevisiae, or budding yeast, is a great model organism for studying the cell cycle because of its rapid growth and well-characterized genetics. Elm1 is a protein kinase in yeast that regulates both the cell cycle and cell shape. This study explores Boi1 and its paralog Boi2 as potential downstream effectors of Elm1, focusing on their roles in cell polarity and septin ring formation. Boi1 and Boi2 localize to septin structures similarly to Cdc14. Cdc14 is part of the Mitotic Exit Network (MEN), which controls the transition from mitosis to G1 and is crucial for septin ring rearrangement. Deletion of BOI1 results in an increased number of cells in the pre-cytokinesis stage, indicating a delay in this cell cycle event. This study examines how Boi1 and Boi2 interact with MEN and influence bud formation and cell regulation. Yeast strains with either single or double deletions of BOI1, BOI2, and ELM1 were created or tagged with GFP for visualization. Using Leica Thunder microscopy, we observed that BOI1 deletion reduced double ring septin formation, suggesting Boi1 promotes it, while BOI2 deletion increased it, indicating Boi2 inhibits it. Both Boi1 and Boi2 influenced the formation of double ring septin structures that are crucial for cytokinesis and displayed distinct localization patterns at the bud neck during the septin ring transition from hourglass to double ring. These findings improve our understanding of septin ring organization and have broader implications for similar processes in other eukaryotic cells.

Competition history

• AJAS 2025 Category not listed

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