Published online 31 October 2005. doi:10.1083/jcb.200504091
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 3, 431-436
Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis
Tomoya Yamaguchi1,
Hidemasa Goto1,
Tomoya Yokoyama1,2,
Herman Silljé3,
Anja Hanisch3,
Andreas Uldschmid3,
Yasushi Takai4,
Takashi Oguri1,
Erich A. Nigg3, and
Masaki Inagaki1
1 Division of Biochemistry, Aichi Cancer Center Research Institute, Aichi 464-8681, Japan
2 Department of Dermatology, Mie University Faculty of Medicine, Mie 514-8507, Japan
3 Department of Cell Biology, Max-Planck Institute for Biochemistry, D-82152 Martinsried, Germany
4 Department of Obstetrics and Gynecology, Saitama Medical Center, Saitama 350-8550, Japan
Correspondence to Masaki Inagaki: minagaki{at}aichi-cc.jp
Abstract
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
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.
Abbreviations used in this paper: CBB, Coomassie brilliant blue; IF, intermediate filament; PBD, Polo-box domain; Plk1, Polo-like kinase 1; PP1, protein phosphatase 1; pS, phosphoserine; pT, phosphothreonine; siRNA, small interference RNA; WT, wild type.

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