TorsinA & LAP1 Proteins are Required for Nuclear Migration

One of the known causes of dystonia is the malfunction of a protein called TorsinA. TorsinA is found in human neurons and other cell types and appears to have a role in multiple cell processes. A team led by DMRF grant recipient G. W. Gant Luxton at University of Minnesota have added a new role to TorsinA’s expanding repertoire.

Experimenting in cell models, he and his team have demonstrated that TorsinA and its activator protein, LAP1, regulate protein complexes that facilitate nuclear migration. Relocating the nucleus of a cell is required for many processes including fertilization, muscle development, and neuronal growth. These experiments used fibroblasts (cells that make up connective tissue), not neurons, so it is unclear at this time how relevant the discoveries may be to dystonia. However, other investigators have discovered fibroblast abnormalities in human dystonia patients, and future experiments with this model may offer a new perspective from which to ultimately clarify TorsinA function.

The study was highlighted by Cell Biology journal with a special introduction by Daniel Starr and Lesilee Rose, a former DMRF grant recipient whose work has contributed important TorsinA findings.

Saunders CA, Harris NJ, Willey PT. TorsinA controls TAN line assembly and the retrograde flow of dorsal perinuclear actin cables during rearward nuclear movement. J Cell Biol. 2017 Mar 6;216(3):657-674. Starr DA, Rose LS. TorsinA regulates the LINC to moving nuclei. Cell Biol. 2017 Mar 6;216(3):543-545.

Last update: May 2017