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Updated: May 24, 2025

Spatiotemporal Analysis of Cytokinetic Events in Fission Yeast
Published on: February 20, 2017
PP2A-B56 regulates Mid1 protein levels for proper cytokinesis in fission yeast
Madeline L Chrupcala1, James B Moseley1
1Department of Biochemistry and Cell Biology, The Geisel School of Medicine at Dartmouth, Hanover, NH.
Abstract:
Protein phosphorylation regulates many steps in the cell division process including cytokinesis. In fission yeast cells, the anillin-like protein Mid1 sets the cell division plane and is regulated by phosphorylation. Multiple protein kinases act on Mid1, but no protein phosphatases have been shown to regulate Mid1. Here, we discovered that the conserved protein phosphatase PP2A-B56 is required for proper cytokinesis by promoting Mid1 protein levels. We find that par1∆ cells lacking the primary B56 subunit divide asymmetrically due to the assembly of misplaced cytokinetic rings that slide toward cell tips. These par1∆ mutants have reduced whole-cell levels of Mid1 protein, leading to reduced Mid1 at the cytokinetic ring. Restoring proper Mid1 expression suppresses par1∆ cytokinesis defects. This work identifies a new PP2A-B56 pathway regulating cytokinesis through Mid1, with implications for control of cytokinesis in other organisms.
Insights
The protein phosphatase PP2A-B56 is crucial for cell division by maintaining Mid1 protein levels. Its absence causes asymmetric cell division due to misplaced cytokinetic rings in fission yeast.
Area of Science:
- Cell Biology
- Molecular Biology
- Genetics
Background:
- Protein phosphorylation regulates cell division, including cytokinesis.
- Mid1, an anillin-like protein, establishes the cell division plane in fission yeast and is regulated by phosphorylation.
- No protein phosphatases were previously known to regulate Mid1.
Purpose of the Study:
- To investigate the role of protein phosphatases in regulating Mid1 and cytokinesis.
- To identify novel regulators of the cell division process.
Main Methods:
- Studied fission yeast mutants lacking the PP2A-B56 subunit (par1∆).
- Assessed cell division, cytokinetic ring assembly, and Mid1 protein levels.
- Investigated the effect of restoring Mid1 expression in par1∆ mutants.
Main Results:
- PP2A-B56 is essential for proper cytokinesis by promoting Mid1 protein levels.
- par1∆ cells exhibit asymmetric division with misplaced cytokinetic rings.
- Reduced Mid1 protein levels in par1∆ mutants lead to defects at the cytokinetic ring.
- Restoring Mid1 expression rescues the cytokinesis defects in par1∆ cells.
Conclusions:
- Identified a novel pathway where PP2A-B56 regulates cytokinesis through Mid1.
- This finding has implications for understanding cytokinesis control in various organisms.
- PP2A-B56 plays a critical role in maintaining Mid1 protein homeostasis for accurate cell division.
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