ArticleCellular and molecular life sciences : CMLS2022
PP2A-Cdc55 phosphatase regulates actomyosin ring contraction and septum formation during cytokinesis.
Article in Cellular and molecular life sciences : CMLS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Synthetic trap-peptides identify a TOM complex phosphatase - PP2A dephosphorylates Tom6.The FEBS journal · 2026Article
- A coordinated kinase and phosphatase network regulates Stu2 recruitment to yeast kinetochores.The Journal of cell biology · 2025Article
- PP2A-B56 regulates Mid1 protein levels for proper cytokinesis in fission yeast.Molecular biology of the cell · 2025Article
- Central Role of the Actomyosin Ring in Coordinating Cytokinesis Steps in Budding Yeast.Journal of fungi (Basel, Switzerland) · 2024Review
- Downregulation of protein phosphatase 2Aα in asthmatic airway smooth muscle.American journal of physiology. Lung cellular and molecular physiology · 2024Article
- Chitin Synthesis in Yeast: A Matter of Trafficking.International journal of molecular sciences · 2022Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Eukaryotic cells divide and separate all their components after chromosome segregation by a process called cytokinesis to complete cell division. Cytokinesis is highly regulated by the recruitment of the components to the division site and through post-translational modifications such as phosphorylations. The budding yeast mitotic kinases Cdc28-Clb2, Cdc5, and Dbf2-Mob1 phosphorylate several cytokinetic proteins contributing to the regulation of cytokinesis. The PP2A-Cdc55 phosphatase regulates mitosis counteracting Cdk1- and Cdc5-dependent phosphorylation. This prompted us to propose that PP2A-Cdc55 could also be counteracting the mitotic kinases during cytokinesis. Here we show that in the absence of Cdc55, AMR contraction and the primary septum formation occur asymmetrically to one side of the bud neck supporting a role for PP2A-Cdc55 in cytokinesis regulation. In addition, by in vivo and in vitro assays, we show that PP2A-Cdc55 dephosphorylates the chitin synthase II (Chs2 in budding yeast) a component of the Ingression Progression Complexes (IPCs) involved in cytokinesis. Interestingly, the non-phosphorylable version of Chs2 rescues the asymmetric AMR contraction and the defective septa formation observed in cdc55∆ mutant cells. Therefore, timely dephosphorylation of the Chs2 by PP2A-Cdc55 is crucial for proper actomyosin ring contraction. These findings reveal a new mechanism of cytokinesis regulation by the PP2A-Cdc55 phosphatase and extend our knowledge of the involvement of multiple phosphatases during cytokinesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.