TY - JOUR
T1 - Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells
AU - Hirota, Toru
AU - Kunitoku, Naoko
AU - Sasayama, Takashi
AU - Marumoto, Tomotoshi
AU - Zhang, Dongwei
AU - Nitta, Masayuki
AU - Hatakeyama, Katsuyoshi
AU - Saya, Hideyuki
N1 - Funding Information:
We are grateful to M. Kimura and Y. Okano (Gifu University) for Aurora-A cDNA. We thank S. Honda, S. Iida, Y. Kawano (Kumamoto University), T. Iwanaga (Hokkaido University), J.-M. Peters, S. Hauf (Institute of Molecular Pathology, Vienna), J. Pines, and M. Jackman (University of Cambridge) for their critical discussions. We thank Y. Fukushima for secretarial assistance, and members of the Gene Technology Center in Kumamoto University for technical supports. This work was supported by grants from the Ministry of Education, Science, Sports, and Culture of Japan and the “Research for the Future” program of The Japan Society for the Promotion of Science (H.S.).
PY - 2003/9/5
Y1 - 2003/9/5
N2 - Aurora family kinases contribute to regulation of mitosis. Using RNA interference in synchronized HeLa cells, we now show that Aurora-A is required for mitotic entry. We found that initial activation of Aurora-A in late G2 phase of the cell cycle is essential for recruitment of the cyclin B1-Cdk1 complex to centrosomes, where it becomes activated and commits cells to mitosis. A two-hybrid screen identified the LIM protein Ajuba as an Aurora-A binding protein. Ajuba and Aurora-A interact in mitotic cells and become phosphorylated as they do so. In vitro analyses revealed that Ajuba induces the autophosphorylation and consequent activation of Aurora-A. Depletion of Ajuba prevented activation of Aurora-A at centrosomes in late G2 phase and inhibited mitotic entry. Overall, our data suggest that Ajuba is an essential activator of Aurora-A in mitotic commitment.
AB - Aurora family kinases contribute to regulation of mitosis. Using RNA interference in synchronized HeLa cells, we now show that Aurora-A is required for mitotic entry. We found that initial activation of Aurora-A in late G2 phase of the cell cycle is essential for recruitment of the cyclin B1-Cdk1 complex to centrosomes, where it becomes activated and commits cells to mitosis. A two-hybrid screen identified the LIM protein Ajuba as an Aurora-A binding protein. Ajuba and Aurora-A interact in mitotic cells and become phosphorylated as they do so. In vitro analyses revealed that Ajuba induces the autophosphorylation and consequent activation of Aurora-A. Depletion of Ajuba prevented activation of Aurora-A at centrosomes in late G2 phase and inhibited mitotic entry. Overall, our data suggest that Ajuba is an essential activator of Aurora-A in mitotic commitment.
UR - https://www.scopus.com/pages/publications/0141429171
UR - https://www.scopus.com/pages/publications/0141429171#tab=citedBy
U2 - 10.1016/S0092-8674(03)00642-1
DO - 10.1016/S0092-8674(03)00642-1
M3 - Article
C2 - 13678582
AN - SCOPUS:0141429171
SN - 0092-8674
VL - 114
SP - 585
EP - 598
JO - Cell
JF - Cell
IS - 5
ER -