A FRET biosensor reveals spatiotemporal activation and functions of aurora kinase A in living cells

Giulia Bertolin, Florian Sizaire, Gaëtan Herbomel, David Reboutier, Claude Prigent and Marc Tramier ()
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Giulia Bertolin: CNRS, UMR 6290
Florian Sizaire: CNRS, UMR 6290
Gaëtan Herbomel: CNRS, UMR 6290
David Reboutier: CNRS, UMR 6290
Claude Prigent: CNRS, UMR 6290
Marc Tramier: CNRS, UMR 6290

Nature Communications, 2016, vol. 7, issue 1, 1-16

Abstract: Abstract Overexpression of AURKA is a major hallmark of epithelial cancers. It encodes the multifunctional serine/threonine kinase aurora A, which is activated at metaphase and is required for cell cycle progression; assessing its activation in living cells is mandatory for next-generation drug design. We describe here a Förster’s resonance energy transfer (FRET) biosensor detecting the conformational changes of aurora kinase A induced by its autophosphorylation on Thr288. The biosensor functionally replaces the endogenous kinase in cells and allows the activation of the kinase to be followed throughout the cell cycle. Inhibiting the catalytic activity of the kinase prevents the conformational changes of the biosensor. Using this approach, we discover that aurora kinase A activates during G1 to regulate the stability of microtubules in cooperation with TPX2 and CEP192. These results demonstrate that the aurora kinase A biosensor is a powerful tool to identify new regulatory pathways controlling aurora kinase A activation.

Date: 2016
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DOI: 10.1038/ncomms12674

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