非洲爪蟾极光-A激酶pEg2中功能性破坏盒的鉴定。

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

作者信息

Arlot-Bonnemains Y, Klotzbucher A, Giet R, Uzbekov R, Bihan R, Prigent C

机构信息

Groupe Cycle Cellulaire, UMR 6061 Génétique et Développement, CNRS-Université de Rennes 1, IFR 97 Génomique Fonctionnelle et Santé, Faculté de Médecine, 2 avenue du Pr Léon Bernard, CS 34317, 35043 Rennes Cedex, France.

出版信息

FEBS Lett. 2001 Nov 9;508(1):149-52. doi: 10.1016/s0014-5793(01)03048-4.

DOI:10.1016/s0014-5793(01)03048-4

PMID:11707286

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.

摘要

与所有极光A激酶一样，非洲爪蟾pEg2激酶水平在G(2)/M期达到峰值，在G(1)期细胞中几乎检测不到，这表明该蛋白在有丝分裂结束时会像人类极光A激酶那样被降解。我们首次在激酶催化结构域的C末端鉴定出一个RxxL序列。将该RxxL序列突变为RxxI可抑制该蛋白的泛素化及其降解。对应于pEg2功能破坏盒的RxxL序列在包括极光A、-B和-C在内的所有极光激酶的整个进化过程中都得到了保守。