A variety of debilitating neuro-degenerative diseases are caused by the defective folding of particular proteins. A case in point is amyotrophic lateral sclerosis (ALS or Lou Gehrig’s disease), which can be caused by the misfolding of superoxide dismutase 1 (SOD1). The misfolded proteins aggregate in the cytosol of motor neurons, eventually causing their death, and thereby the progressive paralyzation characteristic of the disease. Nagy et al. found that overexpression of an Hsp110 protein in motor neurons improved the survival of SOD1 mutant mouse models of ALS. Hsp110 proteins are part of a cytosolic protein disaggregation machinery. Thus, increasing the disaggregation capacity of the cytosol can help to alleviate the progression of a neurodegenerative disease.
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