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

doi:10.1038/sj.onc.1205432

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 journal › Article › peer-review

137 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 language	English
Pages (from-to)	3103-3111
Number of pages	9
Journal	Oncogene
Volume	21
Issue number	20
DOIs	https://doi.org/10.1038/sj.onc.1205432
Publication status	Published - 2002
Externally published	Yes

All Science Journal Classification (ASJC) codes

Molecular Biology
Genetics
Cancer Research

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1038/sj.onc.1205432

Cite this

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title = "Aurora-B associated protein phosphatases as negative regulators of kinase activation",

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.",

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

note = "Funding Information: We thank Dr Tadashi Yamamoto (University of Tokyo, Tokyo) for pME-Gex4T-1 and Ms Tomoko Tsurutome for excellent technical assistance. This work was supported by grants-in-aid for Scientific Research and Core of Excellence from the Ministry of Education, Science, Sports and Culture of Japan.",

year = "2002",

doi = "10.1038/sj.onc.1205432",

language = "English",

volume = "21",

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journal = "Oncogene",

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AU - Sugiyama, Keiichi

AU - Sugiura, Kazumitsu

AU - Hara, Tomohiro

AU - Sugimoto, Kenji

AU - Shima, Hiroshi

AU - Honda, Kei

AU - Furukawa, Koichi

AU - Yamashita, Shunichi

AU - Urano, Takeshi

N1 - Funding Information: We thank Dr Tadashi Yamamoto (University of Tokyo, Tokyo) for pME-Gex4T-1 and Ms Tomoko Tsurutome for excellent technical assistance. This work was supported by grants-in-aid for Scientific Research and Core of Excellence from the Ministry of Education, Science, Sports and Culture of Japan.

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

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SN - 0950-9232

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EP - 3111

JO - Oncogene

JF - Oncogene

IS - 20

ER -

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

Abstract

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UN SDGs

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