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 | |
| Publication status | Published - 22-05-2002 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
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Degradation of human Aurora-A protein kinase is mediated by hCdh1. / Taguchi, Sei ichi; Honda, Kei; Sugiura, Kazumitsu; Yamaguchi, Akio; Furukawa, Koichi; Urano, Takeshi.
In: FEBS Letters, Vol. 519, No. 1-3, 22.05.2002, p. 59-65.Research output: Contribution to journal › Article
TY - JOUR
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
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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UR - http://www.scopus.com/inward/citedby.url?scp=0037157197&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(02)02711-4
DO - 10.1016/S0014-5793(02)02711-4
M3 - Article
C2 - 12023018
AN - SCOPUS:0037157197
VL - 519
SP - 59
EP - 65
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-3
ER -