TorsinA and heat shock proteins act as molecular chaperones: suppression of α-synuclein aggregation

摘要: TorsinA, a protein with homology to yeast heat shock protein104, has previously been demonstrated colocalize α-synuclein in Lewy bodies, the pathological hallmark of Parkinson's disease. Heat proteins are family chaperones that both constitutively expressed and induced by stressors, serve essential functions for refolding and/or degradation. Here, we demonstrate that, like torsinA, specific molecular chaperone bodies. In addition, using cellular model aggregation, torsinA immunopositive inclusions. Further, overexpression suppress aggregation this model, whereas mutant no effect. These data suggest chaperone-like activity disease-associated GAG deletion loss-of-function phenotype. Moreover, these support role proteins, including responses neurodegenerative