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Arresting a Torsin ATPase reshapes the endoplasmic reticulum.

Research paper by April E AE Rose, Chenguang C Zhao, Elizabeth M EM Turner, Anna M AM Steyer, Christian C Schlieker

Indexed on: 28 Nov '13Published on: 28 Nov '13Published in: Journal of Biological Chemistry



Abstract

Torsins are membrane-tethered AAA+ ATPases residing in the nuclear envelope (NE) and endoplasmic reticulum (ER). Here, we show that the induction of a conditional, dominant-negative TorsinB variant provokes a profound reorganization of the endomembrane system into foci containing double membrane structures that are derived from the ER. These double-membrane sinusoidal structures are formed by compressing the ER lumen to a constant width of 15 nm, and are highly enriched in the ATPase activator LULL1. Further, we define an important role for a highly conserved aromatic motif at the C terminus of Torsins. Mutations in this motif perturb LULL1 binding, reduce ATPase activity, and profoundly limit the induction of sinusoidal structures.