The pathogenic human Torsin A in Drosophila activates the unfolded protein response and increases susceptibility to oxidative stress

摘要

BackgroundDystonia1 (DYT1) dystonia is caused by a glutamic acid deletion (ΔE) mutation in the gene encoding Torsin A in humans (HTorA). To investigate the unknown molecular and cellular mechanisms underlying DYT1 dystonia, we performed an unbiased proteomic analysis.