David Kachaner

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Drosophila melanogaster Polo and its human orthologue Polo-like kinase 1 fulfill essential roles during cell division. Members of the Polo-like kinase (Plk) family contain an N-terminal kinase domain (KD) and a C-terminal Polo-Box domain (PBD), which mediates protein interactions. How Plks are regulated in cytokinesis is poorly understood. Here we show that(More)
Entry into mitosis requires the phosphorylation of multiple substrates by cyclin B-Cdk1, while exit from mitosis requires their dephosphorylation, which depends largely on the phosphatase PP2A in complex with its B55 regulatory subunit (Tws in Drosophila). At mitotic entry, cyclin B-Cdk1 activates the Greatwall kinase, which phosphorylates Endosulfine(More)
Mitosis and cytokinesis allow faithful distribution of the duplicated genetic material from one mother to two daughter cells. These cell cycle events are regulated precisely by several kinase families including Cyclin-dependent kinases (CDKs), Aurora kinases and Polo-like kinases (Plks). Interestingly, these proteins are able to collaborate with each other(More)
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