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A more recent version of this article appeared on July 1, 2006
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Submitted on October 3, 2005
Revised on April 11, 2006
Accepted on April 27, 2006
at the G2-M Transition
*Department of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, MN 55455;
Louis Pasteur Center for Medical Research, Department of Molecular Biology, Sakyo-ku, Kyoto 606, Japan
Monitoring Editor: Kerry Bloom
HP1 plays an important role in heterochromatin formation, and undergoes large-scale, progressive dissociation from heterochromatin in prophase cells. However, the mechanisms regulating the dynamic behavior of HP1 are poorly understood. In this study, the role of Aurora-B was investigated with respect to the dynamic behavior of HP1
. Mammalian Aurora-B, AIM-1, colocalizes with HP1
to the heterochromatin in G2. Depletion of Aurora-B/AIM-1 inhibited dissociation of HP1
from the chromosome arms at the G2-M transition. In addition, depletion of INCENP led to aberrant cellular localization of Aurora-B/AIM-1, but did not affect heterochromatin targeting of HP1
. It was proposed in the binary switch hypothesis, that phosphorylation of histone H3 at Ser-10 negatively regulates the binding of HP1
to the adjacent methylated Lys-9. However, Aurora-B/AIM-1-mediated phosphorylation of H3 induced dissociation of the HP1
chromodomain, but not of the intact protein in vitro, indicating that the center and/or C-terminal domain of HP1
interferes with the effect of H3 phosphorylation on HP1
dissociation. Interestingly, Lys-9 methyltransferase SUV39H1 is abnormally localized along the metaphase chromosome arms in Aurora-B/AIM-1 depleted cells. In conclusion, these results showed that Aurora-B/AIM-1 is necessary for regulated histone modifications involved in binding of HP1
by the N-terminus of histone H3 during mitosis.
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