TorsinA, which is mutated in early onset torsion dystonia, is found to assist in the degradation of proteins in a part of the cell called the endoplasmic reticulum. These findings, published in Nature Communications this week, suggest that increased endoplasmic reticulum stress in the neurons of these patients may contribute to the disease.
Xandra Breakefield and colleagues demonstrate a new cellular role for TorsinA in the endoplasmic reticulum and show that TorsinA can protect against endoplasmic reticulum stress in nematode worms that carry a mutant version of a certain cystic fibrosis regulator protein. They also find that fibroblasts from patients with early onset torsion dystonia are more sensitive to pharmacological agents that cause endoplasmic reticulum stress and are less able to degrade the mutant version of the cystic fibrosis regulator protein.
These findings may prompt study of endoplasmic reticulum stress in the neurons of patients with early onset torsion dystonia with the potential of preventing stress in this cell within the patients.