Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication

DOI

10.1083/jcb.200306009

Type

Journal article

Journal

J Cell Biol

Publication Date

01/09/2003

Volume

162

Pages

863 - 875

Keywords

Cell Cycle Proteins, Cell Division, Cyclin B, HeLa Cells, Humans, Inhibitor of Apoptosis Proteins, Kinesin, Microtubule-Associated Proteins, Microtubules, Neoplasm Proteins, Phosphorylation, Protein Binding, Protein Kinases, Protein Structure, Tertiary, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, RNA, Small Interfering, Spindle Apparatus, Tubulin