IDENTIFICATION OF MAJOR NUCLEOLAR PROTEINS AS CANDIDATE MITOTIC SUBSTRATES OF CDC2 KINASE

被引:337
作者
PETER, M
NAKAGAWA, J
DOREE, M
LABBE, JC
NIGG, EA
机构
[1] CNRS,F-34033 MONTPELLIER,FRANCE
[2] INSERM,F-34033 MONTPELLIER,FRANCE
关键词
D O I
10.1016/0092-8674(90)90093-T
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
Following the identification of the cdc2 kinase as a major element controlling entry of cells into mitosis, it is important to define the physiological target range of this enzyme. Here, we demonstrate that two major nucleolar proteins, nucleolin and NO38, are highly phosphorylated during mitosis. Importantly, the two nucleolar proteins are also phosphorylated by highly purified starfish cdc2 kinase in vitro, on sites that correspond to those observed specifically during mitosis in vivo. A repeated motif (TPXKK) is identified as the likely mitotic phosphoacceptor site in nucleolin, in that a synthetic peptide mimicking this site functions as both a substrate and a competitive inhibitor of cdc2 kinase. These results identify two novel candidate substrates for cdc2 kinase, and they implicate protein phosphorylation in controlling mitotic changes in nucleolar structure and activity. © 1990.
引用
收藏
页码:791 / 801
页数:11
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