Identification of a functional destruction box in the Xenopus laevis aurora-A kinase pEg2.

Abstract : Like for all aurora-A kinases, the Xenopus pEg2 kinase level peaks in G(2)/M and is hardly detectable in G(1) cells, suggesting that the protein is degraded upon exit from mitosis as reported for the human aurora-A kinase. We identified for the first time a sequence RxxL in the C-terminal end of the kinase catalytic domain. Mutation of this sequence RxxL to RxxI suppresses the ubiquitination of the protein as well as its degradation. The sequence RxxL corresponding to the pEg2 functional destruction box has been conserved throughout evolution in all aurora kinases including aurora-A, -B and -C.
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FEBS Letters, Wiley, 2001, 508 (1), pp.149-52. 〈10.1016/S0014-5793(01)03048-4〉
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http://www.hal.inserm.fr/inserm-00966222
Contributeur : Claude Prigent <>
Soumis le : mercredi 26 mars 2014 - 12:10:44
Dernière modification le : mercredi 25 juillet 2018 - 10:52:02

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Yannick Arlot-Bonnemains, Andrea Klotzbucher, Régis Giet, Rustem Uzbekov, Réjane Bihan, et al.. Identification of a functional destruction box in the Xenopus laevis aurora-A kinase pEg2.. FEBS Letters, Wiley, 2001, 508 (1), pp.149-52. 〈10.1016/S0014-5793(01)03048-4〉. 〈inserm-00966222〉

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