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

被引：49

作者：

Arlot-Bonnemains, Y ^{[1
]}

Klotzbucher, A ^{[1
]}

Giet, R ^{[1
]}

Uzbekov, R ^{[1
]}

Bihan, R ^{[1
]}

Prigent, C ^{[1
]}

机构：

[1] Univ Rennes 1, Grp Cycle Cellulaire, UMR 6061 Genet & Dev, CNRS,IFR 97 Genom Fonct & Sante,Fac Med, F-35043 Rennes, France

来源：

FEBS LETTERS | 2001年 / 508卷 / 01期

关键词：

aurora-A; proteasome; degradation; Xenopus;

D O I：

10.1016/S0014-5793(01)03048-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Like for all aurora-A kinases, the Xenopus pEg2 kinase level peaks in G(2)/M and is hardly detectable in G, 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. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：149 / 152

页数：4

共 22 条

[1] Cell cycle-regulated proteolysis of mitotic target proteins [J].