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

Research output: Contribution to journalArticlepeer-review

126 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)3103-3111
Number of pages9
JournalOncogene
Volume21
Issue number20
DOIs
Publication statusPublished - 2002
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics
  • Cancer Research

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