Histone deacetylase 3 localizes to the plasma membrane and is a substrate of Src.
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.
Department of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
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Longworth
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Laimins
D000081247:CSK Tyrosine-Protein Kinase; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology*; D006655:Histone Deacetylases / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D011485:Protein Binding; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D013379:Substrate Specificity; D019061:src-Family Kinases; D000099186:Histone Deacetylase 3
D000081247:CSK Tyrosine-Protein Kinase; D006655:Histone Deacetylases; D011505:Protein-Tyrosine Kinases; D019061:src-Family Kinases; D000099186:Histone Deacetylase 3; C000631346:CSK protein, human