Histone deacetylase 3 localizes to the plasma membrane and is a substrate of Src

M. S. Longworth, L. A. Laimins*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

83 Scopus citations

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 languageEnglish (US)
Pages (from-to)4495-4500
Number of pages6
JournalOncogene
Volume25
Issue number32
DOIs
StatePublished - Jul 27 2006

Keywords

  • HDAC3
  • Phosphorylation
  • Plasma membrane
  • Tyrosine
  • c-Src

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cancer Research

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