Journal
JOURNAL OF CELLULAR PHYSIOLOGY
Volume 228, Issue 7, Pages 1525-1535Publisher
WILEY-BLACKWELL
DOI: 10.1002/jcp.24311
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Funding
- Canadian Institutes of Health Research [MOP-9186]
- Canada Research Chair
- MHRC/CancerCare Manitoba studentship
- Austrian Science Fund [FWF P22340]
- GEN-AU project Epigenetic Regulation of cell Fate Decisions (BM: WF)
- FWF
- Austrian Science Fund (FWF) [P 22340] Funding Source: researchfish
- Austrian Science Fund (FWF) [P22340] Funding Source: Austrian Science Fund (FWF)
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During mitosis, histone deacetylase 2 (HDAC2) becomes highly phosphorylated through the action of CK2, and HDAC1 and 2 are displaced from mitotic chromosomes. HDAC1 and 2 are components of corepressor complexes, which function with lysine acetyltransferases to catalyze dynamic protein acetylation and regulate gene expression. In this study, we show that HDAC1 and 2 associate with F-actin in mitotic cells. Inhibition of Aurora B or protein kinase CK2 did not prevent the displacement of HDAC1 and 2 from mitotic chromosomes in HeLa cells. Further, proteins of the HDAC1 and 2 corepressor complexes and transcription factors recruiting these corepressors to chromatin were dissociated from mitotic chromosomes independent of Aurora B activity. HDAC1 and 2 returned to the nuclei of daughter cells during lamin A/C reassembly and before Sp1, Sp3, and RNA polymerase II. Our results show that HDAC1 and 2 corepressor complexes are removed from the mitotic chromosomes and are available early in the events leading to the re-establishment of the gene expression program in daughter cells. J. Cell. Physiol. 228: 15251535, 2013. (c) 2012 Wiley Periodicals, Inc.
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