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HDAC6-p97/VCP controlled polyubiquitin chain turnover.

HDAC6 is a unique cytoplasmic deacetylase capable of interacting with ubiquitin. Using a combination of biophysical, biochemical and biological approaches, we have characterized the ubiquitin-binding domain of HDAC6, named ZnF-UBP, and investigated its biological functions. These studies show that the three Zn ion-containing HDAC6 ZnF-UBP domain presents the highest known affinity for ubiquitin monomers and mediates the ability of HDAC6 to negatively control the cellular polyubiquitin chain turnover. We further show that HDAC6-interacting chaperone, p97/VCP, dissociates the HDAC6-ubiquitin complexes and counteracts the ability of HDAC6 to promote the accumulation of polyubiquitinated proteins. We propose that a finely tuned balance of HDAC6 and p97/VCP concentrations determines the fate of ubiquitinated misfolded proteins: p97/VCP would promote protein degradation and ubiquitin turnover, whereas HDAC6 would favour the accumulation of ubiquitinated protein aggregates and inclusion body formation.

Pubmed ID: 16810319

Authors

  • Boyault C
  • Gilquin B
  • Zhang Y
  • Rybin V
  • Garman E
  • Meyer-Klaucke W
  • Matthias P
  • Müller CW
  • Khochbin S

Journal

The EMBO journal

Publication Data

July 26, 2006

Associated Grants

None

Mesh Terms

  • 3T3 Cells
  • Adenosine Triphosphatases
  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Cell Cycle Proteins
  • Cercopithecus aethiops
  • HeLa Cells
  • Histone Deacetylases
  • Humans
  • Mice
  • Mice, Knockout
  • Molecular Sequence Data
  • Polyubiquitin
  • Protein Folding