Sticking to the nuclear envelope

A mutation in torsinA, an AAA ATPase protein, causes DYT1 dystonia in humans. On page 855, Goodchild and Dauer identify two protein binding partners of torsinA, one that localizes to the ER membrane and one that spans the inner membrane of the nuclear envelope. The team hypothesizes that DYT1 is a nuclear envelope disease, and that identification of such protein complexes will provide a mechanistic probe into a poorly characterized region of the cell.

In wild-type cells, the majority of torsinA protein localizes to the lumen of the ER, while a small proportion associates with the nuclear envelope. In cells carrying the disease-associated mutation, the proportion of torsinA at the envelope increases. Furthermore, a torsinA mutant that cannot hydrolyze ATP, and therefore becomes trapped on its target protein, selectively localizes to the nuclear periphery....