JCB logo
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

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
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 761K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yamaguchi, T.
Right arrow Articles by Inagaki, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yamaguchi, T.
Right arrow Articles by Inagaki, M.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*HomoloGene*UniGene
*Compound via MeSH
*Substance via MeSH
Hazardous Substances DB
*L-SERINE
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Report

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.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents