JCB logo
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 25 August 2003. doi:10.1083/jcb.200306009
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 640K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
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 Neef, R.
Right arrow Articles by Barr, F. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Neef, R.
Right arrow Articles by Barr, F. A.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*HomoloGene*UniGene
*Substance via MeSH
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?

© The Rockefeller University Press, 0021-9525/2003/9/863 $5.00
The Journal of Cell Biology, Volume 162, Number 5, 863-876

Article

Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis



Rüdiger Neef1, Christian Preisinger1, Josephine Sutcliffe1, Robert Kopajtich1, Erich A. Nigg2, Thomas U. Mayer2 and Francis A. Barr1,2

1 Intracellular Protein Transport, Independent Junior Research Group
2 Department of Cell Biology, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany

Address correspondence to Francis Barr, Max-Planck-Institute of Biochemistry, Dept. of Cell Biology, Am Klopferspitz 18a, 82152 Martinsried, Germany. Tel.: 49-89-8578-3135. Fax: 49-89-8578-3102. email: barr{at}biochem.mpg.de

We have investigated the function of mitotic kinesin-like protein (MKlp) 2, a kinesin localized to the central spindle, and demonstrate that its depletion results in a failure of cleavage furrow ingression and cytokinesis, and disrupts localization of polo-like kinase 1 (Plk1). MKlp2 is a target for Plk1, and phosphorylated MKlp2 binds to the polo box domain of Plk1. Plk1 also binds directly to microtubules and targets to the central spindle via its polo box domain, and this interaction controls the activity of Plk1 toward MKlp2. An antibody to the neck region of MKlp2 that prevents phosphorylation of MKlp2 by Plk1 causes a cytokinesis defect when introduced into cells. We propose that phosphorylation of MKlp2 by Plk1 is necessary for the spatial restriction of Plk1 to the central spindle during anaphase and telophase, and the complex of these two proteins is required for cytokinesis.

Key Words: polo kinase; Plk1; MKlp2; central spindle; rabkinesin

The online version of this article includes supplemental material.

J. Sutcliffe's present address is Adolph Butenandt Institut, Lehrstuhl für Molekularbiologie, Schillerstr. 44, 80336 Munich, Germany.

Abbreviations used in this paper: MKlp, mitotic kinesin-like protein; Plk1, polo-like kinase 1; siRNA, small interfering RNA.


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