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J Biol Chem. 2014 Jan 3;289(1):552-64. doi: 10.1074/jbc.M113.515791. Epub 2013 Nov 25.

Arresting a Torsin ATPase reshapes the endoplasmic reticulum.

Author information

1
From the Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520.

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.

KEYWORDS:

AAA+ ATPase; ATPases; Electron Microscopy (EM); Endoplasmic Reticulum(ER); Enzyme Mechanisms; Membrane Structure; Torsin

PMID:
24275647
PMCID:
PMC3879577
DOI:
10.1074/jbc.M113.515791
[Indexed for MEDLINE]
Free PMC Article

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