The DYRK-family kinase Pom1 phosphorylates the F-BAR protein Cdc15 to prevent division at cell poles
| Autor: | Pranav Ullal, Kathleen L. Gould, Rachel H. Roberts-Galbraith, Jun-Song Chen, Libera Lo Presti, Nathan A. McDonald, Sophie G. Martin |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Serine/threonine-specific protein kinase
0303 health sciences Cyclin-dependent kinase 1 biology Cell division Cyclin-dependent kinase 2 Cell Biology Article 3. Good health Pom1 Cell biology 03 medical and health sciences 0302 clinical medicine biology.protein Cyclin-dependent kinase 7 cGMP-dependent protein kinase 030217 neurology & neurosurgery Cytokinesis Research Articles 030304 developmental biology |
| Zdroj: | The Journal of Cell Biology Journal of Cell Biology, vol. 211, no. 3, pp. 653-668 |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | In rod-shaped fission yeast cells, the DYRK-family kinase Pom1, which localizes at cell poles, inhibits the formation of the contractile actomyosin ring at these regions by phosphorylating the key ring component, F-BAR protein Cdc15, allowing the ring to slide toward the middle of the cell. Division site positioning is critical for both symmetric and asymmetric cell divisions. In many organisms, positive and negative signals cooperate to position the contractile actin ring for cytokinesis. In rod-shaped fission yeast Schizosaccharomyces pombe cells, division at midcell is achieved through positive Mid1/anillin-dependent signaling emanating from the central nucleus and negative signals from the dual-specificity tyrosine phosphorylation-regulated kinase family kinase Pom1 at the cell poles. In this study, we show that Pom1 directly phosphorylates the F-BAR protein Cdc15, a central component of the cytokinetic ring. Pom1-dependent phosphorylation blocks Cdc15 binding to paxillin Pxl1 and C2 domain protein Fic1 and enhances Cdc15 dynamics. This promotes ring sliding from cell poles, which prevents septum assembly at the ends of cells with a displaced nucleus or lacking Mid1. Pom1 also slows down ring constriction. These results indicate that a strong negative signal from the Pom1 kinase at cell poles converts Cdc15 to its closed state, destabilizes the actomyosin ring, and thus promotes medial septation. |
| Databáze: | OpenAIRE |
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