[HTML][HTML] Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers
KC Stein, R Bengoechea, MB Harms, CC Weihl… - Journal of Biological …, 2014 - ASBMB
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, which has known …
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, which has known …