Tyrosine phosphorylation of HDAC3 by Src kinase mediates proliferation of HER2‐positive breast cancer cells

(kinase inactive form). When these tyrosine residues are all substituted for alanine residues, the deacetylase activity of mutant HDAC3 was abolished. In addition, a proliferation of HER2-positive breast cancer cells expressing phosphorylation deficient mutant HDAC3 is decreased in comparison with control cells. Thus, our findings suggested that phosphorylation of HDAC3 by c-Src kinase regulates the HDAC3 activity and the proliferation of breast cancer cells.