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Originally published In Press as doi:10.1074/jbc.C200378200 on August 9, 2002

J. Biol. Chem., Vol. 277, Issue 39, 35783-35786, September 27, 2002
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ACCELERATED PUBLICATION
The Transcriptional Repressor Sp3 Is Associated with CK2-phosphorylated Histone Deacetylase 2*

Jian-Min Sun, Hou Yu Chen, Mariko Moniwa, David W. LitchfieldDagger , Edward Seto§, and James R. Davie

From the Manitoba Institute of Cell Biology, Winnipeg, Manitoba R3E 0V9, Canada, Dagger  Department of Biochemistry, University of Western Ontario, London, Ontario N6A 5C1, Canada, and § H. Lee Moffitt Cancer Center and Research Institute, University of South Florida, Tampa, Florida 33612

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 deacetylases (HDACs) 1 and 2. Although most HDAC2 is not phosphorylated in the breast cancer cells, HDAC2 bound to Sp1 and 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 and Sp1 and Sp3 complexes reduced the associated HDAC activity. Protein kinase CK2 is up-regulated 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.

* This research was supported in part by Canadian Institute of Health Research (CIHR) Grant MT-9186 and United States Army Medical and Material Command Breast Cancer Research Program Grant DAMD17-00-1-0319.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Recipient of a CIHR Senior Scientist award. To whom correspondence should be addressed: Manitoba Institute of Cell Biology, 675 McDermot Ave., Winnipeg, Manitoba R3E 0V9, Canada. Tel.: 204-787-2391; Fax: 204-787-2190; E-mail: davie@cc.umanitoba.ca.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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