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

Keiichi Sugiyama, Kazumitsu Sugiura, Tomohiro Hara, Kenji Sugimoto, Hiroshi Shima, Kei Honda, Koichi Furukawa, Shunichi Yamashita, Takeshi Urano

研究成果: ジャーナルへの寄稿学術論文査読

136 被引用数 (Scopus)

抄録

The human serine/threonine kinase Aurora-B is structurally related to the protein kinase Ipl1p 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 1 (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.

本文言語英語
ページ(範囲)3103-3111
ページ数9
ジャーナルOncogene
21
20
DOI
出版ステータス出版済み - 2002
外部発表はい

All Science Journal Classification (ASJC) codes

  • 分子生物学
  • 遺伝学
  • 癌研究

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