TY - JOUR
T1 - Autophosphorylation of a Newly Identified Site of Aurora-B Is Indispensable for Cytokinesis
AU - Yasui, Yoshihiro
AU - Urano, Takeshi
AU - Kawajiri, Aie
AU - Nagata, Koh Ichi
AU - Tatsuka, Masaaki
AU - Saya, Hideyuki
AU - Furukawa, Koichi
AU - Takahashi, Toshitada
AU - Izawa, Ichiro
AU - Inagaki, Masaki
PY - 2004/3/26
Y1 - 2004/3/26
N2 - Mitotic kinases regulate cell division and its checkpoints, errors of which can lead to aneuploidy or genetic instability. One of these is Aurora-B, a key kinase that is required for chromosome alignment at the metaphase plate and for cytokinesis in mammalian cells. We report here that human Aurora-B is phosphorylated at Thr-232 through interaction with the inner centromere protein (INCENP) in vivo. The phosphorylation of Thr-232 occurs by means of an autophosphorylation mechanism, which is indispensable for the Aurora-B kinase activity. The activation of Aurora-B spatio-temporally correlated with the site-specific phosphorylation of its physiological substrates, histone H3 and vimentin. Overexpression of the TA mutant of Aurora-B, in which Thr-232 was changed into alanine, frequently induced multinuclearity in cells. These results indicate that the phosphorylation of Thr-232 is an essential regulatory mechanism for Aurora-B activation.
AB - Mitotic kinases regulate cell division and its checkpoints, errors of which can lead to aneuploidy or genetic instability. One of these is Aurora-B, a key kinase that is required for chromosome alignment at the metaphase plate and for cytokinesis in mammalian cells. We report here that human Aurora-B is phosphorylated at Thr-232 through interaction with the inner centromere protein (INCENP) in vivo. The phosphorylation of Thr-232 occurs by means of an autophosphorylation mechanism, which is indispensable for the Aurora-B kinase activity. The activation of Aurora-B spatio-temporally correlated with the site-specific phosphorylation of its physiological substrates, histone H3 and vimentin. Overexpression of the TA mutant of Aurora-B, in which Thr-232 was changed into alanine, frequently induced multinuclearity in cells. These results indicate that the phosphorylation of Thr-232 is an essential regulatory mechanism for Aurora-B activation.
UR - http://www.scopus.com/inward/record.url?scp=11144354860&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=11144354860&partnerID=8YFLogxK
U2 - 10.1074/jbc.M311128200
DO - 10.1074/jbc.M311128200
M3 - Article
C2 - 14722118
AN - SCOPUS:11144354860
SN - 0021-9258
VL - 279
SP - 12997
EP - 13003
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 13
ER -