Abstract
Histone deacetylases (HDACs) negatively regulate gene expression by removing acetyl groups from lysine residues present in histones and other proteins. Histone deacetylase 3 is unique among the Class I family of HDACs, as it is able to shuttle between the nucleus and the cytoplasm, whereas the other family members remain in the nucleus. Histone deacetylase 3 often forms complexes with corepressor proteins that do not associate with the other Class I HDACs, and its phosphorylation correlates with increased enzymatic activity. Here we show that HDAC3 also localizes to the plasma membrane in multiple cell types. Furthermore, c-Src is shown to form a complex with HDAC3 at the plasma membrane and to use HDAC3 as a substrate for phosphorylation. Our results describe a novel localization and binding partner for the HDAC3 protein, as well as implicate c-Src in HDAC3 regulation.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 4495-4500 |
| Number of pages | 6 |
| Journal | Oncogene |
| Volume | 25 |
| Issue number | 32 |
| DOIs | |
| State | Published - Jul 27 2006 |
Funding
We thank Keith Glaser at Abbott Laboratories for the pcDNA3.1-HDAC3 vector. We thank the members of the Laimins laboratory for advice and comments on protocols. We also thank Dr Ashok Aiyar for his advice and suggestions. MSL was supported by National Cancer Institute Carcinogenesis Training Grant no. T32CA09560. This work was supported by a Sexually Transmitted Diseases Cooperative Research Center grant funded through the National Institute of Allergy and Infectious Diseases.
Keywords
- HDAC3
- Phosphorylation
- Plasma membrane
- Tyrosine
- c-Src
ASJC Scopus subject areas
- Molecular Biology
- Genetics
- Cancer Research