DYRK kinase Pom1 drives F-BAR protein Cdc15 from the membrane to promote medial division
| Autor: | Libera Lo Presti, Nathan A. McDonald, Rachel H. Roberts-Galbraith, Kathleen L. Gould, Rahul Bhattacharjee, Marcin Wos, Chloe E. Snider, Sophie G. Martin, Jun-Song Chen, MariaSanta C. Mangione |
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| Rok vydání: | 2020 |
| Předmět: |
Cell
Cell Cycle Proteins Pom1 GTP-Binding Proteins Schizosaccharomyces medicine Phosphorylation Kinase activity Molecular Biology Paxillin Cytokinesis biology Kinase Cell Cycle Articles Cell Biology biology.organism_classification Cell biology Cytoskeletal Proteins medicine.anatomical_structure Schizosaccharomyces pombe biology.protein Schizosaccharomyces pombe Proteins Protein Kinases Protein Processing Post-Translational |
| Zdroj: | Molecular biology of the cell, vol. 31, no. 9, pp. 917-929 Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| DOI: | 10.1091/mbc.e20-01-0026 |
| Popis: | In many organisms, positive and negative signals cooperate to position the division site for cytokinesis. In the rod-shaped fission yeast Schizosaccharomyces pombe, symmetric division is achieved through anillin/Mid1-dependent positive cues released from the central nucleus and negative signals from the DYRK-family polarity kinase Pom1 at cell tips. Here we establish that Pom1’s kinase activity prevents septation at cell tips even if Mid1 is absent or mislocalized. We also find that Pom1 phosphorylation of F-BAR protein Cdc15, a major scaffold of the division apparatus, disrupts Cdc15’s ability to bind membranes and paxillin, Pxl1, thereby inhibiting Cdc15’s function in cytokinesis. A Cdc15 mutant carrying phosphomimetic versions of Pom1 sites or deletion of Cdc15 binding partners suppresses division at cell tips in cells lacking both Mid1 and Pom1 signals. Thus, inhibition of Cdc15-scaffolded septum formation at cell poles is a key Pom1 mechanism that ensures medial division. |
| Databáze: | OpenAIRE |
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