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. 2003 Mar 7;278(10):8526-30.
doi: 10.1074/jbc.M210892200. Epub 2002 Nov 27.

Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process

Hidemasa Goto  1 , Yoshihiro Yasui, Aie Kawajiri, Erich A Nigg, Yasuhiko Terada, Masaaki Tatsuka, Koh-ichi Nagata, Masaki Inagaki
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Free article

Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process

Hidemasa Goto et al. J Biol Chem. .
Free article

Abstract

Aurora-B is an evolutionally conserved protein kinase that regulates several mitotic events including cytokinesis. We previously demonstrated the possible existence of a protein kinase that phosphorylates at least Ser-72 on vimentin, the most widely expressed intermediate filament protein, in the cleavage furrow-specific manner. Here we showed that vimentin-Ser-72 phosphorylation occurred specifically at the border of the Aurora-B-localized area from anaphase to telophase. Expression of a dominant-negative mutant of Aurora-B led to a reduction of this vimentin-Ser-72 phosphorylation. In vitro analyses revealed that Aurora-B phosphorylates vimentin at approximately 2 mol phosphate/mol of substrate for 30 min and that this phosphorylation dramatically inhibits vimentin filament formation. We further identified eight Aurora-B phosphorylation sites, including Ser-72 on vimentin, and then constructed the mutant vimentin in which these identified sites are changed into Ala. Cells expressing this mutant formed an unusually long bridge-like intermediate filament structure between unseparated daughter cells. We then identified important phosphorylation sites for the bridge phenotype. Our findings indicate that Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation and controls vimentin filament segregation in cytokinetic process.

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