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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 function and the basis for neuronal dysfunction in DYT1 remain unknown. A clue to disease pathogenesis is the fact that...

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Identifiers

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

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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 ↗

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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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