Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis

Tomoya Yamaguchi, Hidemasa Goto, Tomoya Yokoyama, Herman Silljé, Anja Hanisch, Andreas Uldschmid, Yasushi Takai, Takashi Oguri, Erich A. Nigg, Masaki Inagaki

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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.

Original languageEnglish
Pages (from-to)431-6
Number of pages6
JournalJournal of Cell Biology
Issue number3
Publication statusPublished - 7-Nov-2005
Externally publishedYes


  • 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

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