Role in Cytokinesis
The Aurora B complex is necessary for cytokinesis in vertebrates, C. elegans, Drosophila, and fission yeast.
In various cell types, overexpression of a catalytically inactive Aurora B prevents cytokinesis. Disruption of cytokinesis can also arise from Aurora B mislocalization due to mutation of Aurora B binding partners.
Aurora B targets a number of proteins that localize to the cleavage furrow, including the type-III intermediate filament proteins vimentin, desmin, and glial fibrillary acidic protein (GFAP). In general, phosphorylation destabilizes intermediate filaments. Therefore, it has been proposed that phosphorylation of intermediate filaments at the cleavage furrow destabilizes the filaments in preparation for cytokinesis. In agreement with this hypothesis, mutation of Aurora B target sites in intermediate filament proteins leads to defects in filament deformation and prevents the final stage of cytokinesis.
Aurora B also phosphorylates myosin II regulatory light chain at the cleavage furrow. Inhibition of Aurora B activity prevents proper myosin II localization to the cleavage furrow and disrupts spindle midzone organization.
Read more about this topic: Aurora B Kinase
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