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http://purl.uniprot.org/citations/24275647http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24275647http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24275647http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m113.515791"xsd:string
http://purl.uniprot.org/citations/24275647http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m113.515791"xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/author"Zhao C."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/author"Zhao C."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/author"Schlieker C."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/author"Schlieker C."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/author"Rose A.E."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/author"Rose A.E."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/author"Steyer A.M."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/author"Steyer A.M."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/author"Turner E.M."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/author"Turner E.M."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/pages"552-564"xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/pages"552-564"xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/title"Arresting a Torsin ATPase reshapes the endoplasmic reticulum."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/title"Arresting a Torsin ATPase reshapes the endoplasmic reticulum."xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/volume"289"xsd:string
http://purl.uniprot.org/citations/24275647http://purl.uniprot.org/core/volume"289"xsd:string