| Literature DB >> 12023018 |
Sei ichi Taguchi1, Kei Honda, Kazumitsu Sugiura, Akio Yamaguchi, Koichi Furukawa, Takeshi Urano.
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.Entities:
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Year: 2002 PMID： 12023018 DOI： 10.1016/s0014-5793(02)02711-4
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124