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First published online 15 June 2004
doi: 10.1242/jcs.01173
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Research Article |
1 Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA
2 Department of Genetics, Cell Biology and Development, University of Minnesota, 6-160 Jackson Hall, 321 Church Street, Minneapolis, MN 55455, USA
* Author for correspondence (e-mail: liu13{at}fas.harvard.edu)
Accepted 24 February 2004
Polo-like kinases and kinesin-like motor proteins are among the many proteins implicated in the execution of cytokinesis. Polo-like-kinase 1 (Plk1) interacts with the mitotic kinesin-like motor protein CHO1/MKLP-1 during anaphase and telophase, and CHO1/MKLP-1 is a Plk1 substrate in vitro. Here, we explore the molecular interactions of these two key contributors to mitosis and cytokinesis. Using the transient transfection approach, we show that the C-terminus of Plk1 binds CHO1/MKLP-1 in a Polo-box-dependent manner and that the stalk domain of CHO1/MKLP-1 is responsible for its binding to Plk1. The stalk domain was found to localize with Plk1 to the mid-body, and Plk1 appears to be mislocalized in CHO1/MKLP-1-depleted cells during late mitosis. We showed that Ser904 and Ser905 are two major Plk1 phosphorylation sites. Using the vector-based RNA interference approach, we showed that depletion of CHO1/MKLP-1 causes the formation of multinucleate cells with more centrosomes, probably because of a defect in the early phase of cytokinesis. Overexpression of a non-Plk1-phosphorylatable CHO1 mutant caused cytokinesis defects, presumably because of dominant negative effect of the construct. Finally, CHO1-depletion-induced multinucleation could be partially rescued by co-transfection of a non-degradable hamster wild-type CHO1 construct, but not an unphosphorylatable mutant. These data provide more detailed information about the interaction between Plk1 and CHO1/MKLP-1, and the significance of this is discussed.
Key words: Plk1, CHO1/MKLP-1, Cytokinesis, Interaction
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