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Article

The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein.

The Journal of cell biology - 14 Mar 2005

Goodchild Rose E, Dauer William T

Abstract excerpt

A glutamic acid deletion (DeltaE) in the AAA+ protein torsinA causes DYT1 dystonia. Although the majority of torsinA resides within the endoplasmic reticulum (ER), torsinA binds a substrate in the lumen of the nuclear envelope (NE), and the DeltaE mutation enhances this interaction. Using a novel...

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Identifiers

PMID: 15767459
DOI: 10.1083/jcb.200411026
PMCID: PMC2171781

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-15767459-2026-09-01.1. 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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The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein.PMID 15767459Read ↗

Printor, a novel torsinA-interacting protein implicated in dystonia pathogenesis.Semantic proximity Read ↗

A unique redox-sensing sensor II motif in TorsinA plays a critical role in nucleotide and partner binding.Semantic proximity Read ↗

How lamina-associated polypeptide 1 (LAP1) activates Torsin.Semantic proximity Read ↗

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

The role of torsinA in dystonia.Semantic proximity Read ↗

Regulation of Torsin ATPases by LAP1 and LULL1Semantic proximity Read ↗

TorsinA and dystonia: from nuclear envelope to synapseSemantic proximity Read ↗

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

The nuclear envelope localization of DYT1 dystonia torsinA-ΔE requires the SUN1 LINC complex component.Semantic proximity Read ↗

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

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

The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Semantic proximity Read ↗

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