Article

DYT-TOR1A Subcellular Proteomics Reveals Selective Vulnerability of the Nuclear Proteome to Cell Stress

2021-07-11

Abstract excerpt

TorsinA is a AAA + ATPase that shuttles between the ER lumen and outer nuclear envelope in an ATP-dependent manner and is functionally implicated in nucleocytoplasmic transport. We hypothesized that the DYT-TOR1A dystonia disease-causing variant, ΔE TorsinA, may therefore disrupt the normal subcellular distribution of proteins between the nuclear and cytosolic compartments. To test this hypothesis, we performed p...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 90667b4c-4d4f-52c9-9671-a20a68dac3ad
DOI: 10.1101/2021.07.10.451533

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

DYT-TOR1A Subcellular Proteomics Reveals Selective Vulnerability of the Nuclear Proteome to Cell StressDOI 10.1101/2021.07.10.451533Read

Disruption of Protein Processing in the Endoplasmic Reticulum of DYT1 Knock-in Mice Implicates Novel Pathways in Dystonia Pathogenesis.Semantic proximity Read

Dysregulated nuclear Lamin B1 in DYT1 dystonia thickens the nuclear lamina and disrupts 14-3-3 proteinsSemantic proximity Read

DYT-TOR1A dystonia: an update on pathogenesis and treatmentSemantic proximity Read

Aberrant cellular behavior of mutant torsinA implicates nuclear envelope dysfunction in DYT1 dystonia.Semantic proximity Read

Mislocalization to the nuclear envelope: an effect of the dystonia-causing torsinA mutation.Semantic proximity Read

Biochemical and cellular analysis of human variants of the DYT1 dystonia protein, TorsinA/TOR1A.Semantic proximity Read

Consequences of the DYT1 mutation on torsinA oligomerization and degradation.Semantic proximity Read

TorsinA and dystonia: from nuclear envelope to synapseSemantic proximity Read

The role of torsinA in dystonia.Semantic proximity Read

Disease modeling with human neurons reveals LMNB1 dysregulation underlying DYT1 dystoniaSemantic proximity Read

Mutant torsinA, responsible for early-onset torsion dystonia, forms membrane inclusions in cultured neural cells.Semantic proximity Read

Dystonia-associated TorsinA-ΔE mutation induces a gain-of-function interaction with XPO1 via its N-terminal hydrophobic segmentSemantic proximity Read