Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers.

@article{Stein2014MyopathycausingMI,
  title={Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers.},
  author={Kevin C. Stein and Roc{\'i}o Bengoechea and Matthew B. Harms and Conrad Chris Weihl and Heather L True},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 30},
  pages={21120-30}
}
The molecular chaperone network protects against the toxic misfolding and aggregation of proteins. Disruption of this network leads to a variety of protein conformational disorders. One such example recently discovered is limb-girdle muscular dystrophy type 1D (LGMD1D), which is caused by mutation of the HSP40 chaperone DNAJB6. All LGMD1D-associated mutations localize to the conserved G/F domain of DNAJB6, but the function of this domain is largely unknown. Here, we exploit the yeast HSP40 Sis1… CONTINUE READING