Polo kinase interacts with RacGAP50C and is required to localize the cytokinesis initiation complex

Saman Ebrahimi, Hamilton Fraval, Michael Jacqueline Murray, Robert B. Saint, Stephen L. Gregory

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

The assembly and constriction of an actomyosin contractile ring in cytokinesis is dependent on the activation of Rho at the equatorial cortex by a complex, here termed the cytokinesis initiation complex, between a microtubule-associated kinesin-like protein (KLP), a member of the RacGAP family, and the RhoGEF Pebble. Recently, the activity of the mammalian Polo kinase ortholog Plk1 has been implicated in the formation of this complex. We show here that Polo kinase interacts directly with the cytokinesis initiation complex by binding RacGAP50C. We find that a new domain of Polo kinase, termed the intermediate domain, interacts directly with RacGAP50C and that Polo kinase is essential for localization of the KLP-RacGAP centralspindlin complex to the cell equator and spindle midzone. In the absence of Polo kinase, RacGAP50C and Pav-KLP fail to localize normally, instead decorating microtubules along their length. Our results indicate that Polo kinase directly binds the conserved cytokinesis initiation complex and is required to trigger centralspindlin localization as a first step in cytokinesis.

Original languageEnglish
Pages (from-to)28667-28673
Number of pages7
JournalJournal of Biological Chemistry
Volume285
Issue number37
DOIs
Publication statusPublished - 10 Sep 2010

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