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Science 20 June 2008:
Vol. 320. no. 5883, pp. 1655 - 1658
DOI: 10.1126/science.1157425

Reports

Bora and the Kinase Aurora A Cooperatively Activate the Kinase Plk1 and Control Mitotic Entry

Akiko Seki,1 Judith A. Coppinger,2 Chang-Young Jang,1 John R. Yates, III,2 Guowei Fang1*

A central question in the study of cell proliferation is, what controls cell-cycle transitions? Although the accumulation of mitotic cyclins drives the transition from the G2 phase to the M phase in embryonic cells, the trigger for mitotic entry in somatic cells remains unknown. We report that the synergistic action of Bora and the kinase Aurora A (Aur-A) controls the G2-M transition. Bora accumulates in the G2 phase and promotes Aur-A–mediated activation of Polo-like kinase 1 (Plk1), leading to the activation of cyclin-dependent kinase 1 and mitotic entry. Mechanistically, Bora interacts with Plk1 and controls the accessibility of its activation loop for phosphorylation and activation by Aur-A. Thus, Bora and Aur-A control mitotic entry, which provides a mechanism for one of the most important yet ill-defined events in the cell cycle.

1 Department of Biological Sciences, Stanford University, Stanford, CA 94305–5020, USA.
2 Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037, USA.

* To whom correspondence should be addressed. E-mail: gwfang{at}stanford.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Sequestration of Polo kinase to microtubules by phosphopriming-independent binding to Map205 is relieved by phosphorylation at a CDK site in mitosis.
V. Archambault, P. P. D'Avino, M. J. Deery, K. S. Lilley, and D. M. Glover (2008)
Genes & Dev. 22, 2707-2720
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Science. ISSN 0036-8075 (print), 1095-9203 (online)