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MBC in Press, published online ahead of print January 17, 2007
Mol. Biol. Cell 10.1091/mbc.E06-12-1152

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Submitted on December 29, 2006
Accepted on January 8, 2007

Functional Interaction of Aurora-A and PP2A during Mitosis

Virginie Horn,* Jacques Thélu,* Alphonse Garcia,{dagger} Corinne Albigès-Rizo,* Marc R. Block,* and Jean Viallet*

*Institut Albert Bonniot, Centre de Recherche Institut National de la Santé et de la Recherche Médicale, Université Joseph Fourier U 823, Equipe DySAD, Université Joseph Fourier Site Santé, BP 170, F38042, Grenoble Cedex 09, France; {dagger}Equipe Phosphatase, Unité de Chimie Organique, Institut Pasteur, 75724 Paris Cedex, France

Monitoring Editor: John Pringle

Entry into mitosis is a highly regulated process, promoted by the activated Cyclin B1/Cdk1 complex. Activation of this complex is controlled, in part, by the protein kinase Aurora-A, which is a member of a multigenic serine/threonine kinase family. In normal cells, Aurora-A activity is regulated, at least in part, by degradation through the APC-ubiquitin-proteasome pathway. It has recently been proposed that, in Xenopus, Aurora-A degradation can be inhibited by phosphorylation. It would thus be expected that a phosphatase activity would release this blockade at the end of mitosis. Here, we have shown that the protein phosphatase PP2A and Aurora-A are colocalized at the cell poles during mitosis in human cells and interact within the same complex. Using the PP2A inhibitor okadaic acid and an RNAi approach, we have shown that this interaction is functional within the cell. PP2A/Aurora-A interaction is promoted by an S51D mutation in Aurora-A and inhibited by a phosphomimetic peptide centered around Aurora-A S51, thereby strongly suggesting that PP2A controls Aurora-A degradation by dephosphorylating serine 51 in the A box of the human enzyme.

Address correspondence to: Marc R. Block (marc.block{at}ujf-grenoble.fr)






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