Cdk1 phosphorylation of fission yeast paxillin inhibits its cytokinetic ring localization
| Autor: | MariaSanta C. Mangione, Jun-Song Chen, Kathleen L. Gould |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Mitosis
Cell Cycle Proteins macromolecular substances environment and public health Dephosphorylation CDC2 Protein Kinase Schizosaccharomyces Phosphorylation Molecular Biology Cytokinesis Cyclin-dependent kinase 1 biology Cdc14 Actomyosin Cell Biology biology.organism_classification Actins Cyclin-Dependent Kinases Cell biology Cytoskeletal Proteins enzymes and coenzymes (carbohydrates) Mitotic exit Schizosaccharomyces pombe Brief Reports Schizosaccharomyces pombe Proteins Paxillin biological phenomena cell phenomena and immunity |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| DOI: | 10.1091/mbc.e20-12-0807 |
| Popis: | Divisions of the genetic material and cytoplasm are coordinated spatially and temporally to ensure genome integrity. This coordination is mediated in part by the major cell cycle regulator cyclin-dependent kinase (Cdk1). Cdk1 activity peaks during mitosis, but during mitotic exit/cytokinesis Cdk1 activity is reduced, and phosphorylation of its substrates is reversed by various phosphatases including Cdc14, PP1, PP2A, and PP2B. Cdk1 is known to phosphorylate several components of the actin- and myosin-based cytokinetic ring (CR) that mediates division of yeast and animal cells. Here we show that Cdk1 also phosphorylates the Schizosaccharomyces pombe CR component paxillin Pxl1. We determined that both the Cdc14 phosphatase Clp1 and the PP1 phosphatase Dis2 contribute to Pxl1 dephosphorylation at mitotic exit, but PP2B/calcineurin does not. Preventing Pxl1 phosphorylation by Cdk1 results in increased Pxl1 levels, precocious Pxl1 recruitment to the division site, and increased duration of CR constriction. In vitro Cdk1-mediated phosphorylation of Pxl1 inhibits its interaction with the F-BAR domain of the cytokinetic scaffold Cdc15, thereby disrupting a major mechanism of Pxl1 recruitment. Thus, Pxl1 is a novel substrate through which S. pombe Cdk1 and opposing phosphatases coordinate mitosis and cytokinesis. |
| Databáze: | OpenAIRE |
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