| First Author | Boyault C | Year | 2006 |
| Journal | EMBO J | Volume | 25 |
| Issue | 14 | Pages | 3357-66 |
| PubMed ID | 16810319 | Mgi Jnum | J:111173 |
| Mgi Id | MGI:3653156 | Doi | 10.1038/sj.emboj.7601210 |
| Citation | Boyault C, et al. (2006) HDAC6-p97/VCP controlled polyubiquitin chain turnover. EMBO J 25(14):3357-66 |
| abstractText | 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. |
