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Dynamic distribution of HDAC1 and HDAC2 during mitosis: Association with F‐actin
Author(s) -
He Shihua,
Khan Dilshad H.,
Winter Stefan,
Seiser Christian,
Davie James R.
Publication year - 2013
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.24311
Subject(s) - mitosis , hdac1 , microbiology and biotechnology , biology , corepressor , histone deacetylase 2 , chromatin , histone , genetics , histone deacetylase , gene expression , gene , repressor
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: 1525–1535, 2013. © 2012 Wiley Periodicals, Inc.