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Gene Review

HDAC7  -  histone deacetylase 7

Homo sapiens

Synonyms: DKFZP586J0917, HD7, HD7A, HD7a, HDAC7A, ...
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High impact information on HDAC7A

  • We show that histone deacetylase 7 (HDAC7) is specifically expressed in the vascular endothelium during early embryogenesis, where it maintains vascular integrity by repressing the expression of matrix metalloproteinase (MMP) 10, a secreted endoproteinase that degrades the extracellular matrix [1].
  • Disruption of the HDAC7 gene in mice results in embryonic lethality due to a failure in endothelial cell-cell adhesion and consequent dilatation and rupture of blood vessels [1].
  • Myosin phosphatase dephosphorylates HDAC7, controls its nucleocytoplasmic shuttling, and inhibits apoptosis in thymocytes [2].
  • After T-cell receptor (TCR) activation, the serine/threonine kinase PKD1 phosphorylates HDAC7, resulting in its nuclear export and the derepression of its target genes [2].
  • Inhibition of HDAC7 expression by RNA interference causes increased apoptosis in response to TCR activation [3].

Biological context of HDAC7A

  • Consistent with this hypothesis, the overexpression of Tip60 represses STAT3-driven reporter gene expression, which can be further potentiated by the co-transfection of HDAC7 [4].
  • More importantly, a mutant of HDAC7 specifically deficient in phosphorylation by PKD, inhibits TCR-mediated apoptosis of T cell hybridomas [5].
  • AR acetylation at Lys630/632/633 was not the target of HDAC7 repression, since repression of AR function was independent of these acetylation sites [6].
  • Histone deacetylase 7 (HDAC7) is a member of class IIa HDACs that regulate myocyte enhancer factor-2 (MEF2)-mediated transcription and participate in multiple cellular processes such as T cell apoptosis [7].
  • A highly conserved domain in the N-terminal region of HDAC5 and HDAC7 as well as the zinc finger region of BCL6 were found necessary for the complex formation in vivo and in vitro [8].

Associations of HDAC7A with chemical compounds

  • We identify four serine residues in the NH(2) terminus of HDAC7 as targets for PKD [5].
  • HDAC7 mutations that prevent the interaction with 14-3-3 proteins also block calyculin A-mediated stabilization [9].
  • In sum, our results identify HDAC7 as a novel AR corepressor whose subcellular and subnuclear compartmentalization can be regulated in an androgen-selective manner [6].
  • In the presence of testosterone, a portion of HDAC7 localized to pearl-like nuclear domains, whereas AR occupied with antagonistic ligands cyproterone acetate- or casodex (bicalutamide) recruited HDAC7 from these domains to colocalize with the receptor in speckles and nucleoplasm in a more complete fashion [6].
  • The o-nitrophenyl beta-d-galactopyranoside assay revealed that regions containing amino acids 735-785 of HIF-1alpha and amino acids 669-952 of HDAC7 were minimum contact sites of the interaction [10].

Other interactions of HDAC7A

  • This is the first demonstration of which Tip60 represses STAT3 activity in part through the recruitment of HDAC7 [4].


  1. Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10. Chang, S., Young, B.D., Li, S., Qi, X., Richardson, J.A., Olson, E.N. Cell (2006) [Pubmed]
  2. Myosin phosphatase dephosphorylates HDAC7, controls its nucleocytoplasmic shuttling, and inhibits apoptosis in thymocytes. Parra, M., Mahmoudi, T., Verdin, E. Genes Dev. (2007) [Pubmed]
  3. HDAC7, a thymus-specific class II histone deacetylase, regulates Nur77 transcription and TCR-mediated apoptosis. Dequiedt, F., Kasler, H., Fischle, W., Kiermer, V., Weinstein, M., Herndier, B.G., Verdin, E. Immunity (2003) [Pubmed]
  4. Tip60 is a co-repressor for STAT3. Xiao, H., Chung, J., Kao, H.Y., Yang, Y.C. J. Biol. Chem. (2003) [Pubmed]
  5. Phosphorylation of histone deacetylase 7 by protein kinase D mediates T cell receptor-induced Nur77 expression and apoptosis. Dequiedt, F., Van Lint, J., Lecomte, E., Van Duppen, V., Seufferlein, T., Vandenheede, J.R., Wattiez, R., Kettmann, R. J. Exp. Med. (2005) [Pubmed]
  6. Androgen receptor regulates nuclear trafficking and nuclear domain residency of corepressor HDAC7 in a ligand-dependent fashion. Karvonen, U., Jänne, O.A., Palvimo, J.J. Exp. Cell Res. (2006) [Pubmed]
  7. {alpha}-Actinin 4 Potentiates Myocyte Enhancer Factor-2 Transcription Activity by Antagonizing Histone Deacetylase 7. Chakraborty, S., Reineke, E.L., Lam, M., Li, X., Liu, Y., Gao, C., Khurana, S., Kao, H.Y. J. Biol. Chem. (2006) [Pubmed]
  8. Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor. Lemercier, C., Brocard, M.P., Puvion-Dutilleul, F., Kao, H.Y., Albagli, O., Khochbin, S. J. Biol. Chem. (2002) [Pubmed]
  9. Phosphorylation of the histone deacetylase 7 modulates its stability and association with 14-3-3 proteins. Li, X., Song, S., Liu, Y., Ko, S.H., Kao, H.Y. J. Biol. Chem. (2004) [Pubmed]
  10. Histone deacetylase 7 associates with hypoxia-inducible factor 1alpha and increases transcriptional activity. Kato, H., Tamamizu-Kato, S., Shibasaki, F. J. Biol. Chem. (2004) [Pubmed]
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