HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination

Oncogene. 2007 Aug 13;26(37):5468-76. doi: 10.1038/sj.onc.1210614.


Histone deacetylase 6 (HDAC6) is a unique enzyme with specific structural and functional features. It is actively or stably maintained in the cytoplasm and is the only member, within the histone deacetylase family, that harbors a full duplication of its deacetylase homology region followed by a specific ubiquitin-binding domain at the C-terminus end. Accordingly, this deacetylase functions at the heart of a cellular regulatory mechanism capable of coordinating various cellular functions largely relying on the microtubule network. Moreover, HDAC6 action as a regulator of the HSP90 chaperone activity adds to the multifunctionality of the protein, and allows us to propose a critical role for HDAC6 in mediating and coordinating various cellular events in response to different stressful stimuli.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylation
  • Animals
  • Cell Nucleus / enzymology
  • Cytoskeleton / enzymology*
  • Enzyme Inhibitors / therapeutic use
  • Histone Deacetylase Inhibitors
  • Histone Deacetylases / chemistry
  • Histone Deacetylases / metabolism*
  • Humans
  • Protein Processing, Post-Translational*
  • Protein Structure, Tertiary
  • Signal Transduction
  • Ubiquitin / metabolism*


  • Enzyme Inhibitors
  • Histone Deacetylase Inhibitors
  • Ubiquitin
  • Histone Deacetylases