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

Research output: Contribution to journal › Article › peer-review

92 Citations (Scopus)

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.

Original language	English
Pages (from-to)	59-65
Number of pages	7
Journal	FEBS Letters
Volume	519
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(02)02711-4
Publication status	Published - 22-05-2002
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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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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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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ER -

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

Abstract

All Science Journal Classification (ASJC) codes

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