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Vol. 13, Issue 4, 1099-1108, April 2002
and
*Department of Physiology, University of Massachusetts Medical
School, Worcester, Massachusetts 01605; and Aurora B is a protein kinase and a chromosomal passenger protein
that undergoes dynamic redistribution during mitosis. We have probed
the mechanism that regulates its localization with cells expressing
green fluorescent protein (GFP)-tagged wild-type or mutant aurora B. Aurora B was found at centromeres at prophase and persisted until
~0.5 min after anaphase onset, when it redistributed to the spindle
midzone and became concentrated at the equator along midzone
microtubules. Depolymerization of microtubules inhibited the
dissociation of aurora B from centromeres at early anaphase and caused
the dispersion of aurora B from the spindle midzone at late anaphase;
however, centromeric association during prometaphase was unaffected.
Inhibition of CDK1 deactivation similarly caused aurora B to remain
associated with centromeres during anaphase. In contrast, inhibition of
the kinase activity of aurora B appeared to have no effect on its
interactions with centromeres or initial relocation onto midzone
microtubules. Instead, kinase-inactive aurora B caused abnormal mitosis
and deactivation of the spindle checkpoint. In addition, midzone
microtubule bundles became destabilized and aurora B dispersed from the
equator. Our results suggest that microtubules, CDK1, and the kinase
activity each play a distinct role in the dynamics and functions of
aurora B in dividing cells.
Department of
Regulatory Radiobiology, Research Institute for Radiation Biology and
Medicine, Hiroshima University, Hiroshima 734-8553, Japan
Corresponding author. E-mail
address: yuli.wang{at}umassmed.edu.
Online version of this
article contains video material for some figures. Online version
available at www.molbiolcell.org.
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