A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation.

@article{Hageman2010ADC,
  title={A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation.},
  author={J. Hageman and M. Rujano and M. A. van Waarde and Vaishali Kakkar and R. Dirks and N. Govorukhina and Henderika M. J. Oosterveld-Hut and N. Lubsen and H. Kampinga},
  journal={Molecular cell},
  year={2010},
  volume={37 3},
  pages={
          355-69
        }
}
Misfolding and aggregation are associated with cytotoxicity in several protein folding diseases. A large network of molecular chaperones ensures protein quality control. Here, we show that within the Hsp70, Hsp110, and Hsp40 (DNAJ) chaperone families, members of a subclass of the DNAJB family (particularly DNAJB6b and DNAJB8) are superior suppressors of aggregation and toxicity of disease-associated polyglutamine proteins. The antiaggregation activity is largely independent of the N-terminal… Expand
HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones.
Suppression of protein aggregation by chaperone modification of high molecular weight complexes
HDAC inhibitors and chaperone function.
DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios
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