Abstract
The chromosomal passenger complex consisting of Borealin, INCENP, Survivin, and Aurora B follows a dynamic pattern of localization to perform its role as a regulator of chromosome alignment, aspects of the spindle assembly checkpoint, and cytokinesis. Post-translational modifications of chromosomal passenger proteins play an important role in regulating the localization and function of the complex. Borealin displays a slower electrophoretic mobility during mitosis as a result of phosphorylation. Here we show that phosphorylation at S219 is responsible for this mobility shift. An S219A mutant of Borealin that cannot be phosphorylated at this site displays a defect in centromere localization that is evident in cells arrested in mitosis with nocodazole. Further, the S219A form of Borealin is unable to efficiently rescue mitotic defects that occur upon knock-down of the endogenous protein. These defects are correlated with a reduction in the intensity of Mad2 staining at kinetochores in cells expressing the S219A form of Borealin. These results highlight an important role for phosphorylation of Borealin at S219 in the proper progression through mitosis.