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Journal Article

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

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78193

Kawajiri,  A.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Goto, H., Yasui, Y., Kawajiri, A., Nigg, E. A., Terada, Y., Tatsuka, M., et al. (2003). Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process. Journal of Biological Chemistry, 278(10), 8526-8530.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6C77-5
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 similar to2 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.