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Vol. 17, Issue 7, 3232-3241, July 2006

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Aurora-B/AIM-1 Regulates the Dynamic Behavior of HP1 at the G₂–M Transition

Yasuhiko Terada^*,

*Department of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, MN 55455; and Department of Molecular Biology, Louis Pasteur Center for Medical Research, Kyoto 606, Japan

Submitted October 3, 2005; Revised April 11, 2006; Accepted April 27, 2006
Monitoring Editor: Kerry Bloom

Heterochromatin protein 1 (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 it 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 together 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.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Address correspondence to: Yasuhiko Terada ( terad002{at}tc.umn.edu)

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