被撤回的出版物: The DYRK-family kinase Pornl phosphorylates the F-BAR protein Cdc15 to prevent division at cell poles(Retracted article. See vol. 216, 2017)

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 Poml 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. Poml -dependent phosphorylation blocks Cdcl 5 binding to paxillin Pxl1 and C2 domain protein Ficl and enhances Cdcl 5 dynamics. This promotes ring sliding from cell poles, which prevents septum assembly at the ends of cells with a displaced nucleus or lacking Mid 1. Pom 1 also slows down ring constriction. These results indicate that a strong negative signal from the Poml kinase at cell poles converts Cdc15 to its closed state, destabilizes the actomyosin ring, and thus promotes medial septation.