Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosisYamaguchi, T., Goto, H., Yokoyama, T., Silljé, H., Hanisch, A., Uldschmid, A., Takai, Y., Oguri, T., Nigg, E. A. & Inagaki, M., 7-Nov-2005, In : Journal of Cell Biology. 171, 3, p. 431-6 6 p.
Research output: Contribution to journal › Article › Academic › peer-review
Several kinases phosphorylate vimentin, the most common intermediate filament protein, in mitosis. Aurora-B and Rho-kinase regulate vimentin filament separation through the cleavage furrow-specific vimentin phosphorylation. Cdk1 also phosphorylates vimentin from prometaphase to metaphase, but its significance has remained unknown. Here we demonstrated a direct interaction between Plk1 and vimentin-Ser55 phosphorylated by Cdk1, an event that led to Plk1 activation and further vimentin phosphorylation. Plk1 phosphorylated vimentin at approximately 1 mol phosphate/mol substrate, which partly inhibited its filament forming ability, in vitro. Plk1 induced the phosphorylation of vimentin-Ser82, which was elevated from metaphase and maintained until the end of mitosis. This elevation followed the Cdk1-induced vimentin-Ser55 phosphorylation, and was impaired by Plk1 depletion. Mutational analyses revealed that Plk1-induced vimentin-Ser82 phosphorylation plays an important role in vimentin filaments segregation, coordinately with Rho-kinase and Aurora-B. Taken together, these results indicated a novel mechanism that Cdk1 regulated mitotic vimentin phosphorylation via not only a direct enzyme reaction but also Plk1 recruitment to vimentin.
|Number of pages||6|
|Journal||Journal of Cell Biology|
|Publication status||Published - 7-Nov-2005|
- Actin Cytoskeleton, Amino Acid Motifs, Animals, Aurora Kinase B, Aurora Kinases, CDC2 Protein Kinase, Catalysis, Cell Cycle Proteins, Cell Line, Cytokinesis, Humans, Mice, Mitosis, Mutation, Phosphorylation, Protein Binding, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, Serine, Vimentin, rho GTP-Binding Proteins