부산대학교 도서관

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.bbrc.2007.06.167 Byline: Paulina Karwowska-Desaulniers, Anastasia Ketko, Nayana Kamath, Mary Kay H. Pflum Keywords: Histone deacetylase; HDAC1; Protein phosphorylation Abstract: Histone Deacetylase 1 (HDAC1) is a transcriptional regulator associated with proliferation, apoptosis, and tumorigenesis, although its precise cellular role is unclear. HDAC1 was previously characterized as a phosphoprotein where mutation of phosphorylated S421 and S423 resulted in a loss of deacetylase activity and protein association. Here, the role of phosphorylation in regulating HDAC1 function was examined using phospho-specific antibodies. The antibody studies revealed that phosphorylation at S421 and S423 is constant during the cell cycle, under stress conditions, or in the presence of kinase or phosphatase inhibitors. Further, phosphorylation is dispensable for catalysis or protein association in vitro, as revealed by phosphatase studies. Truncation mutants of HDAC1 demonstrated that binding to Sin3A is promoted by S421 and S423 phosphorylation, while interaction with RbAp48 is not. Taken together, the data are consistent with constitutive phosphorylation of HDAC1 at S421 and S423 in vivo, which is dispensable for activity in vitro. Author Affiliation: Department of Chemistry, Wayne State University, 5101 Cass Avenue, Detroit, MI 48202, USA Article History: Received 29 June 2007 Article Note: (footnote) [star] This work was supported by the National Institutes of Health (GM067657) and Wayne State University.