Abstract
Spinobulbar muscular atrophy (SBMA) is caused by an expansion of a CAG repeat in the androgen receptor (AR), resulting in a polyglutamine tract in the AR. Wang et al. showed that overexpression of heat shock protein 70 (HSP70)-interacting protein (HIP), a chaperone that promotes binding of HSP70 to its substrates, promoted the clearance of polyglutamine AR in vitro. They identified a compound that acted similarly to HIP (by allosterically promoting HSP70 binding to unfolded substrates) and reduced toxicity in a fruitfly model of SBMA.
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