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Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis

Yamaguchi, 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

APA

Yamaguchi, T., Goto, H., Yokoyama, T., Silljé, H., Hanisch, A., Uldschmid, A., Takai, Y., Oguri, T., Nigg, E. A., & Inagaki, M. (2005). Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis. Journal of Cell Biology, 171(3), 431-6. https://doi.org/10.1083/jcb.200504091

Author

Yamaguchi, Tomoya ; Goto, Hidemasa ; Yokoyama, Tomoya ; Silljé, Herman ; Hanisch, Anja ; Uldschmid, Andreas ; Takai, Yasushi ; Oguri, Takashi ; Nigg, Erich A. ; Inagaki, Masaki. / Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis. In: Journal of Cell Biology. 2005 ; Vol. 171, No. 3. pp. 431-6.

Harvard

Yamaguchi, T, Goto, H, Yokoyama, T, Silljé, H, Hanisch, A, Uldschmid, A, Takai, Y, Oguri, T, Nigg, EA & Inagaki, M 2005, 'Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis', Journal of Cell Biology, vol. 171, no. 3, pp. 431-6. https://doi.org/10.1083/jcb.200504091

Standard

Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis. / Yamaguchi, Tomoya; Goto, Hidemasa; Yokoyama, Tomoya; Silljé, Herman; Hanisch, Anja; Uldschmid, Andreas; Takai, Yasushi; Oguri, Takashi; Nigg, Erich A.; Inagaki, Masaki.

In: Journal of Cell Biology, Vol. 171, No. 3, 07.11.2005, p. 431-6.

Research output: Contribution to journal › Article › Academic › peer-review

Vancouver

Yamaguchi T, Goto H, Yokoyama T, Silljé H, Hanisch A, Uldschmid A et al. Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis. Journal of Cell Biology. 2005 Nov 7;171(3):431-6. https://doi.org/10.1083/jcb.200504091

BibTeX

@article{8d23f17fced041b39ff29b5271c90991,
title = "Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis",
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 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.",
keywords = "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",
author = "Tomoya Yamaguchi and Hidemasa Goto and Tomoya Yokoyama and Herman Sillj{\'e} and Anja Hanisch and Andreas Uldschmid and Yasushi Takai and Takashi Oguri and Nigg, {Erich A.} and Masaki Inagaki",
year = "2005",
month = nov,
day = "7",
doi = "10.1083/jcb.200504091",
language = "English",
volume = "171",
pages = "431--6",
journal = "The Journal of Cell Biology",
issn = "0021-9525",
publisher = "ROCKEFELLER UNIV PRESS",
number = "3",

}

RIS

TY - JOUR

T1 - Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis

AU - Yamaguchi, Tomoya

AU - Goto, Hidemasa

AU - Yokoyama, Tomoya

AU - Silljé, Herman

AU - Hanisch, Anja

AU - Uldschmid, Andreas

AU - Takai, Yasushi

AU - Oguri, Takashi

AU - Nigg, Erich A.

AU - Inagaki, Masaki

PY - 2005/11/7

Y1 - 2005/11/7

N2 - 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.

AB - 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.

KW - Actin Cytoskeleton

KW - Amino Acid Motifs

KW - Animals

KW - Aurora Kinase B

KW - Aurora Kinases

KW - CDC2 Protein Kinase

KW - Catalysis

KW - Cell Cycle Proteins

KW - Cell Line

KW - Cytokinesis

KW - Humans

KW - Mice

KW - Mitosis

KW - Mutation

KW - Phosphorylation

KW - Protein Binding

KW - Protein-Serine-Threonine Kinases

KW - Proto-Oncogene Proteins

KW - Serine

KW - Vimentin

KW - rho GTP-Binding Proteins

U2 - 10.1083/jcb.200504091

DO - 10.1083/jcb.200504091

M3 - Article

C2 - 16260496

VL - 171

SP - 431

EP - 436

JO - The Journal of Cell Biology

JF - The Journal of Cell Biology

SN - 0021-9525

IS - 3

ER -

ID: 15139681

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