Journal
JOURNAL OF CELL BIOLOGY
Volume 207, Issue 2, Pages 201-211Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201408081
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Funding
- Canadian Institutes of Health Research (CIHR)
- Natural Sciences and Engineering Research Council of Canada
- CIHR
- Fonds de recherche du Quebec - Sante (FRQS)
- Cole Foundation
- Bettencourt Schueller Foundation
- FRQS
- Canadian Center of Excellence in Commercialization and Research (CECR)
- Canada Foundation for Innovation (CFI)
- CFI
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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 phosphorylation of Polo by Aurora B is required for cytokinesis. This phosphorylation in the activation loop of the KD promotes the dissociation of Polo from the PBD-bound microtubule-associated protein Map205, which acts as an allosteric inhibitor of Polo kinase activity. This mechanism allows the release of active Polo from microtubules of the central spindle and its recruitment to the site of cytokinesis. Failure in Polo phosphorylation results in both early and late cytokinesis defects. Importantly, the antagonistic regulation of Polo by Aurora B and Map205 in cytokinesis reveals that interdomain allosteric mechanisms can play important roles in controlling the cellular functions of Plks.
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