Premium
Degradation of human Aurora‐A protein kinase is mediated by hCdh1
Author(s) -
Taguchi Sei-ichi,
Honda Kei,
Sugiura Kazumitsu,
Yamaguchi Akio,
Furukawa Koichi,
Urano Takeshi
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02711-4
Subject(s) - cdc20 , anaphase promoting complex , microbiology and biotechnology , proteasome , f box protein , ubiquitin , aurora a kinase , skp1 , biology , mitosis , ubiquitin ligase , cell cycle protein , cyclin dependent kinase 7 , drosophila melanogaster , protein kinase a , kinase , biochemistry , map kinase kinase kinase , anaphase , cell cycle , gene
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.