Degradation of human Aurora-A protein kinase is mediated by hCdh1

Sei ichi Taguchi; Kei Honda; Kazumitsu Sugiura; Akio Yamaguchi; Koichi Furukawa; Takeshi Urano

doi:10.1016/S0014-5793(02)02711-4

Degradation of human Aurora-A protein kinase is mediated by hCdh1

Sei ichi Taguchi, Kei Honda, Kazumitsu Sugiura, Akio Yamaguchi, Koichi Furukawa, Takeshi Urano

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

92 被引用数 (Scopus)

抄録

Human Aurora-A is related to a protein kinase originally identified by its close homology to Ipl1p from Saccharomyces cerevisiae and aurora from Drosophila melanogaster, which are key regulators of the structure and function of the mitotic spindle. We previously showed that human Aurora-A is turned over through the anaphase promoting complex/cyclosome (APC/C)-ubiquitin-proteasome pathway. The association of two distinct WD40 repeat proteins known as Cdc20 and Cdh1, respectively, sequentially activates the APC/C. The present study shows that Aurora-A degradation is dependent on hCdh1 in vivo, not on hCdc20, and that Aurora-A is targeted for proteolysis through distinct structural features of the destruction box, the KEN box motifs and its kinase activity.

本文言語	英語
ページ（範囲）	59-65
ページ数	7
ジャーナル	FEBS Letters
巻	519
号	1-3
DOI	https://doi.org/10.1016/S0014-5793(02)02711-4
出版ステータス	出版済み - 22-05-2002
外部発表	はい

All Science Journal Classification (ASJC) codes

生物理学
構造生物学
生化学
分子生物学
遺伝学
細胞生物学

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10.1016/S0014-5793(02)02711-4

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title = "Degradation of human Aurora-A protein kinase is mediated by hCdh1",

abstract = "Human Aurora-A is related to a protein kinase originally identified by its close homology to Ipl1p from Saccharomyces cerevisiae and aurora from Drosophila melanogaster, which are key regulators of the structure and function of the mitotic spindle. We previously showed that human Aurora-A is turned over through the anaphase promoting complex/cyclosome (APC/C)-ubiquitin-proteasome pathway. The association of two distinct WD40 repeat proteins known as Cdc20 and Cdh1, respectively, sequentially activates the APC/C. The present study shows that Aurora-A degradation is dependent on hCdh1 in vivo, not on hCdc20, and that Aurora-A is targeted for proteolysis through distinct structural features of the destruction box, the KEN box motifs and its kinase activity.",

author = "Taguchi, {Sei ichi} and Kei Honda and Kazumitsu Sugiura and Akio Yamaguchi and Koichi Furukawa and Takeshi Urano",

note = "Funding Information: We thank 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.",

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T1 - Degradation of human Aurora-A protein kinase is mediated by hCdh1

AU - Taguchi, Sei ichi

AU - Honda, Kei

AU - Sugiura, Kazumitsu

AU - Yamaguchi, Akio

AU - Furukawa, Koichi

AU - Urano, Takeshi

N1 - Funding Information: We thank 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 - 2002/5/22

Y1 - 2002/5/22

N2 - Human Aurora-A is related to a protein kinase originally identified by its close homology to Ipl1p from Saccharomyces cerevisiae and aurora from Drosophila melanogaster, which are key regulators of the structure and function of the mitotic spindle. We previously showed that human Aurora-A is turned over through the anaphase promoting complex/cyclosome (APC/C)-ubiquitin-proteasome pathway. The association of two distinct WD40 repeat proteins known as Cdc20 and Cdh1, respectively, sequentially activates the APC/C. The present study shows that Aurora-A degradation is dependent on hCdh1 in vivo, not on hCdc20, and that Aurora-A is targeted for proteolysis through distinct structural features of the destruction box, the KEN box motifs and its kinase activity.

AB - Human Aurora-A is related to a protein kinase originally identified by its close homology to Ipl1p from Saccharomyces cerevisiae and aurora from Drosophila melanogaster, which are key regulators of the structure and function of the mitotic spindle. We previously showed that human Aurora-A is turned over through the anaphase promoting complex/cyclosome (APC/C)-ubiquitin-proteasome pathway. The association of two distinct WD40 repeat proteins known as Cdc20 and Cdh1, respectively, sequentially activates the APC/C. The present study shows that Aurora-A degradation is dependent on hCdh1 in vivo, not on hCdc20, and that Aurora-A is targeted for proteolysis through distinct structural features of the destruction box, the KEN box motifs and its kinase activity.

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JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

Degradation of human Aurora-A protein kinase is mediated by hCdh1

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