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HDAC6-p97/VCP controlled polyubiquitin chain turnover.

The EMBO journal | Jul 26, 2006

http://www.ncbi.nlm.nih.gov/pubmed/16810319

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 RIS Download

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

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