Autophosphorylation of a Newly Identified Site of Aurora-B Is Indispensable for Cytokinesis

Yoshihiro Yasui, Takeshi Urano, Aie Kawajiri, Koh Ichi Nagata, Masaaki Tatsuka, Hideyuki Saya, Koichi Furukawa, Toshitada Takahashi, Ichiro Izawa, Masaki Inagaki

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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.

Original languageEnglish
Pages (from-to)12997-13003
Number of pages7
JournalJournal of Biological Chemistry
Issue number13
Publication statusPublished - 2004 Mar 26
Externally publishedYes


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Yasui, Y., Urano, T., Kawajiri, A., Nagata, K. I., Tatsuka, M., Saya, H., Furukawa, K., Takahashi, T., Izawa, I., & Inagaki, M. (2004). Autophosphorylation of a Newly Identified Site of Aurora-B Is Indispensable for Cytokinesis. Journal of Biological Chemistry, 279(13), 12997-13003.