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HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo.

Microtubules are cylindrical cytoskeletal structures found in almost all eukaryotic cell types which are involved in a great variety of cellular processes. Reversible acetylation on the epsilon-amino group of alpha-tubulin Lys40 marks stabilized microtubule structures and may contribute to regulating microtubule dynamics. Yet, the enzymes catalysing this acetylation/deacetylation have remained unidentified until recently. Here we report that beta-tubulin interacts with histone deacetylase-6 (HDAC-6) in a yeast two-hybrid assay and in vitro. We find that HDAC-6 is a micro tubule-associated protein capable of deacetylating alpha-tubulin in vivo and in vitro. HDAC-6's microtubule binding and deacetylation functions both depend on the hdac domains. Overexpression of HDAC-6 in mammalian cells leads to tubulin hypoacetylation. In contrast, inhibition of HDAC-6 function by two independent mechanisms--pharmacological (HDAC inhibitors) or genetic (targeted inactivation of HDAC-6 in embryonic stem cells)--leads to hyperacetylation of tubulin and microtubules. Taken together, our data provide evidence that HDAC-6 might act as a dual deacetylase for tubulin and histones, and suggest the possibility that acetylated non-histone proteins might represent novel targets for pharmacological therapy by HDAC inhibitors.

Pubmed ID: 12606581


  • Zhang Y
  • Li N
  • Caron C
  • Matthias G
  • Hess D
  • Khochbin S
  • Matthias P


The EMBO journal

Publication Data

March 3, 2003

Associated Grants


Mesh Terms

  • 3T3 Cells
  • Acetylation
  • Animals
  • Cattle
  • Chromatography, High Pressure Liquid
  • Embryo, Mammalian
  • Histone Deacetylases
  • Humans
  • Kidney
  • Mice
  • Microtubules
  • Paclitaxel
  • Peptides
  • Protein Binding
  • Protein Structure, Tertiary
  • Stem Cells
  • Tubulin
  • Two-Hybrid System Techniques