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

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 - 09-05-2002
Externally published	Yes

All Science Journal Classification (ASJC) codes

Molecular Biology
Genetics
Cancer Research

UN SDGs

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

Access to Document

10.1038/sj/onc/1205432

Cite this

@article{19d6fd2add0445b8994c0de791cda228,

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",

year = "2002",

month = may,

day = "9",

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

language = "English",

volume = "21",

pages = "3103--3111",

journal = "Oncogene",

issn = "0950-9232",

publisher = "Springer Nature",

number = "20",

}

TY - JOUR

T1 - Aurora-B associated protein phosphatases as negative regulators of kinase activation

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

PY - 2002/5/9

Y1 - 2002/5/9

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.

UR - http://www.scopus.com/inward/record.url?scp=0037046504&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037046504&partnerID=8YFLogxK

U2 - 10.1038/sj/onc/1205432

DO - 10.1038/sj/onc/1205432

M3 - Article

C2 - 12082625

SN - 0950-9232

VL - 21

SP - 3103

EP - 3111

JO - Oncogene

JF - Oncogene

IS - 20

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this