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Papers In Press, published online ahead of print August 9, 2002
J. Biol. Chem, 10.1074/jbc.C200378200
Submitted on June 25, 2002
Revised on August 7, 2002
Accepted on August 9, 2002
Manitoba Institute of Cell Biology, University of Manitoba, Winnipeg, Manitoba R3E OV9
Corresponding Author: davie{at}cc.umanitoba.ca
Sp1 and Sp3 are ubiquitously expressed mammalian transcription factors that function as activators or repressors. Although both transcription factors share a common domain involved in forming multimers, we demonstrate that Sp1 and Sp3 form separate complexes in estrogen dependent human breast cancer cells. Sp1 and Sp3 complexes associate with histone deacetylase (HDAC) 1 and HDAC2. Although most HDAC2 is not phosphorylated in the breast cancer cells, HDAC2 bound to Sp1, Sp3 and cross-linked to chromatin in situ is highly enriched in a phosphorylated form that has a reduced mobility in SDS polyacrylamide gels. We show that protein kinase CK2 is associated with and phosphorylates HDAC2. Alkaline phosphatase treatment of HDAC2, Sp1 and Sp3 complexes reduced the associated HDAC activity. Protein kinase CK2 is upregulated in several cancers including breast cancer, and Sp1 and Sp3 have key roles in estrogen-induced proliferation and gene expression in estrogen-dependent breast cancer cells. CK2 phosphorylation of HDAC2 recruited by Sp1 or Sp3 could regulate HDAC activity and alter the balance of histone deacetylase and histone acetyltransferase activities and dynamic chromatin remodeling of estrogen regulated genes.
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