Aurora-B associated protein phosphatases as negative regulators of kinase activation

被引：125

作者：

Sugiyama, K

Sugiura, K

Hara, T

Sugimoto, K

Shima, H

Honda, K

Furukawa, K

Yamashita, S

Urano, T

机构：

[1] Nagoya Univ, Sch Med, Dept Biochem 2, Showa Ku, Nagoya, Aichi 4660065, Japan

[2] Nagasaki Univ, Sch Med, Dept Nat Med, Atom Bomb Dis Inst, Nagasaki 8528523, Japan

[3] Osaka Prefecture Univ, Div Appl Biochem, Grad Sch Agr & Biol Sci, Sakai, Osaka 5998531, Japan

[4] Hokkaido Univ, Div Biochem Oncol & Immunol, Inst Med Genet, Kita Ku, Sapporo, Hokkaido 0600815, Japan

来源：

ONCOGENE | 2002年 / 21卷 / 20期

关键词：

Aurora-B; historic H3; protein phosphatase; okadaic acid; substrate specificity;

D O I：

10.1038/sj.onc.1205432

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：

The human serine/threonine kinase Aurora-B is structurally related to the protein kinase Ip11p from S cerevisiae and aurora from Drosophila melanogaster, which are key regulators of mitosis. The present study shows that human Aurora-B is activated by okadaic acid and forms complexes with the protein serine/threonine phosphatase type I (PP1) or PP2A, but not with PP5. These data identified Aurora-B associated protein phosphatases as negative regulators of kinase activation. We then used a series of substrates based on a histone H3 phosphorylation site (residues 5-15) to determine the substrate specificity of human Aurora-B. We found that this enzyme is an arginine-directed kinase that can phosphorylate histone H3 at serines 10 and 28 in vitro, suggesting that human Aurora-B is a mitotic histone H3 kinase.

引用

页码：3103 / 3111

页数：9

共 42 条

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