Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the fission yeast DYRK kinase Pom1

Data from ProteomeXchange, PXD ID:PXD001649 . File: o53292.mzml. Published as part of Mol Cell Proteomics. 2015 Feb 26 . From the Abstract: {{i}} ... Here, we sought to determine the phosphorylation targets of Pom1 kinase activity by SILAC-based phosphoproteomics. We defined a set of high-confidence Pom1 targets that were enriched for cytoskeletal and cell growth functions. Cdr2 was the only cell cycle target of Pom1 kinase activity that we identified in cells. Mutation of Pom1-dependent phosphorylation sites in the C-terminus of Cdr2 inhibited mitotic entry but did not impair Cdr2 localization. In addition, we found that Pom1 phosphorylated multiple substrates that function in polarized cell growth, including Tea4, Mod5, Pal1, the Rho GAP Rga7, and the Arf GEF Syt22 ... {{/i}}