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Theses

Mise en evidence et caractérisation d'une interaction fonctionnelle entre la kinase Aurora-A et la phosphatase PP2A

Abstract : Mitosis progression is tightly controlled by a succession of enzymatic reactions, including
those catalyzed by numerous protein kinases and phosphatases. More specifically, the mitotic
serine/threonine kinase Aurora-A is required in these processes as it is involved in the
regulation of the G2/M transition, centrosome cycle, mitotic spindle and chromosomes
segregation. Aurora-A is activated by interacting with other proteins such as TPX2 or AJUBA
and its kinase activity is modulated by the phosphorylation at specific sites. Besides, it has
been recently shown in vitro that Aurora-A degradation by the proteasome pathway is
induced by the dephosphorylation of a highly conserved residue: serine 51. In this study, we
have shown that the phosphatase PP2A and the kinase Aurora-A are co-localized in
centrosomes and are interacting within the same complex. Moreover, the pharmacological
inhibition of PP2A activity or the inhibition of its expression both led to Aurora-A
stabilization in vivo. These results indicate that PP2A controls Aurora-A degradation in vivo.
Finally, we confirmed in vivo in mammalian cells that phosphorylation of the S51 residue
prevents the degradation of Aurora-A.
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https://tel.archives-ouvertes.fr/tel-00138435
Contributor : Virginie Horn <>
Submitted on : Monday, March 26, 2007 - 11:43:48 AM
Last modification on : Friday, November 6, 2020 - 4:11:23 AM
Long-term archiving on: : Wednesday, April 7, 2010 - 12:33:33 AM

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  • HAL Id : tel-00138435, version 1

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CNRS | UJF | U823 | UGA

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Virginie Horn. Mise en evidence et caractérisation d'une interaction fonctionnelle entre la kinase Aurora-A et la phosphatase PP2A. Biologie cellulaire. Université Joseph-Fourier - Grenoble I, 2005. Français. ⟨tel-00138435⟩

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