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Bora and the Kinase Aurora A Cooperatively Activate the Kinase Plk1 and Control Mitotic Entry
Akiko Seki,1Judith A. Coppinger,2Chang-Young Jang,1John R. Yates, III,2Guowei Fang1*
A central question in the study of cell proliferation is, whatcontrols cell-cycle transitions? Although the accumulation ofmitotic cyclins drives the transition from the G2 phase to theM phase in embryonic cells, the trigger for mitotic entry insomatic cells remains unknown. We report that the synergisticaction of Bora and the kinase Aurora A (Aur-A) controls theG2-M transition. Bora accumulates in the G2 phase and promotesAur-A–mediated activation of Polo-like kinase 1 (Plk1),leading to the activation of cyclin-dependent kinase 1 and mitoticentry. Mechanistically, Bora interacts with Plk1 and controlsthe accessibility of its activation loop for phosphorylationand activation by Aur-A. Thus, Bora and Aur-A control mitoticentry, which provides a mechanism for one of the most importantyet 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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Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a.
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122, 1334-1341
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185, 193-202
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Mol. Cell. Biol.
29, 1059-1071
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H. Zhu, J. A. Coppinger, C.-Y. Jang, J. R. Yates III, and G. Fang (2008)
J. Cell Biol.
183, 835-848
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Sequestration of Polo kinase to microtubules by phosphopriming-independent binding to Map205 is relieved by phosphorylation at a CDK site in mitosis.
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