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Article

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

The Journal of neuroscience : the official journal of the Society for Neuroscience - 17 Mar 2004

Gonzalez-Alegre Pedro, Paulson Henry L

Abstract excerpt

Torsion dystonia-1 (DYT1) dystonia, the most common inherited form of dystonia, is caused by a three base pair deletion that eliminates a single amino acid from the disease protein, torsinA. TorsinA is an "AAA" protein thought to reside in the endoplasmic reticulum (ER), yet both its cellular fun...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 15028751
DOI: 10.1523/JNEUROSCI.4461-03.2004
PMCID: PMC6729521

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-15028751-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

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Aberrant cellular behavior of mutant torsinA implicates nuclear envelope dysfunction in DYT1 dystonia.PMID 15028751Read ↗

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

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

Loss of the dystonia-associated protein torsinA selectively disrupts the neuronal nuclear envelope.Semantic proximity Read ↗

LULL1 retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutation.Semantic proximity Read ↗

Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics.Semantic proximity Read ↗

The role of torsinA in dystonia.Semantic proximity Read ↗

Inhibition of N-linked glycosylation prevents inclusion formation by the dystonia-related mutant form of torsinA.Semantic proximity Read ↗

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Relative tissue expression of homologous torsinB correlates with the neuronal specific importance of DYT1 dystonia-associated torsinASemantic proximity Read ↗

Effect of torsinA on membrane proteins reveals a loss of function and a dominant-negative phenotype of the dystonia-associated DeltaE-torsinA mutant.Semantic proximity Read ↗

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