Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis

被引:115
作者
Yamaguchi, T
Goto, H
Yokoyama, T
Silljé, H
Hanisch, A
Uldschmid, A
Takai, Y
Oguri, T
Nigg, EA
Inagaki, M [1 ]
机构
[1] Aichi Canc Ctr, Res Inst, Div Biochem, Nagoya, Aichi 4648681, Japan
[2] Mie Univ, Fac Med, Dept Dermatol, Tsu, Mie 5148507, Japan
[3] Max Planck Inst Biochem, Dept Cell Biol, D-82152 Martinsried, Germany
关键词
D O I
10.1083/jcb.200504091
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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 similar to 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.
引用
收藏
页码:431 / 436
页数:6
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