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Originally published as MBC in Press, 10.1091/mbc.E02-09-0612 on December 7, 2002
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Vol. 14, Issue 4, 1489-1500, April 2003

Functional Significance of the Specific Sites Phosphorylated in Desmin at Cleavage Furrow: Aurora-B May Phosphorylate and Regulate Type III Intermediate Filaments during Cytokinesis Coordinatedly with Rho-kinase

Aie Kawajiri,*dagger Yoshihiro Yasui,* Hidemasa Goto,* Masaaki Tatsuka,Dagger Masahide Takahashi,dagger Koh-ichi Nagata,* and Masaki Inagaki*§

 *Division of Biochemistry, Aichi Cancer Center Research Institute, Chikusa-ku, Nagoya 464-8681, Japan;  dagger Department of Pathology, Graduate School of Medicine, Nagoya University, Showa-ku, Nagoya 466-8550, Japan; and  Dagger Department of Regulatory Radiobiology, Research Institute for Radiation Biology and Medicine, Hiroshima University, Minami-ku, Hiroshima 734-8553, Japan

Aurora-B is a protein kinase required for chromosome segregation and the progression of cytokinesis during the cell cycle. We report here that Aurora-B phosphorylates GFAP and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by Aurora-B; Thr-7/Ser-13/Ser-38 of GFAP, and Thr-16 of desmin are common with those related to Rho-associated kinase (Rho-kinase), which has been reported to phosphorylate GFAP and desmin at cleavage furrow during cytokinesis. We identified Ser-59 of desmin to be a specific site phosphorylated by Aurora-B in vitro. Use of an antibody that specifically recognized desmin phosphorylated at Ser-59 led to the finding that the site is also phosphorylated specifically at the cleavage furrow during cytokinesis in Saos-2 cells. Desmin mutants, in which in vitro phosphorylation sites by Aurora-B and/or Rho-kinase are changed to Ala or Gly, cause dramatic defects in filament separation between daughter cells in cytokinesis. The results presented here suggest the possibility that Aurora-B may regulate cleavage furrow-specific phosphorylation and segregation of type III IFs coordinatedly with Rho-kinase during cytokinesis.

§ Corresponding author. E-mail address: minagaki{at}aichi-cc.jp.

Molecular Biology of the Cell
Vol. 14, 1489-1500, April 2003
Copyright © 2003 by The American Society for Cell Biology


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