Article

The AAA+ ATPase TorsinA polymerizes into hollow tubes with a helical periodicity of 8.5 subunits per turn

2019-03-04

Abstract excerpt

TorsinA is an ER-resident AAA+ ATPase, whose single residue deletion of glutamate E303 results in the genetic neuromuscular disease primary dystonia. TorsinA is a highly unusual AAA+ ATPase in that it needs an external activator. Also, it appears not to thread a peptide substrate through a narrow central channel, in contrast to its closest structural homologs. Here, we examined the oligomerization of TorsinA to ge...

Topics

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

Identifiers and source

Literature Corpus work: 264125b5-6315-5008-bffe-1490a41db8e1
DOI: 10.1101/567099

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

The AAA+ ATPase TorsinA polymerizes into hollow tubes with a helical periodicity of 8.5 subunits per turnDOI 10.1101/567099Read

The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn.Semantic proximity Read

Dystonia-associated forms of torsinA are deficient in ATPase activity.Semantic proximity Read

Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia.Semantic proximity Read

Torsins: not your typical AAA+ ATPases.Semantic proximity Read

The role of torsinA in dystonia.Semantic proximity Read

TorsinA and dystonia: from nuclear envelope to synapseSemantic proximity Read

The luminal AAA+ ATPase torsinA mediates distinct mechanisms of nuclear-cytoplasmic communication by adopting different functional assembly statesSemantic proximity Read

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

Torsin ATPases: structural insights and functional perspectives.Semantic proximity Read

Regulation of Torsin ATPases by LAP1 and LULL1Semantic proximity Read

Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1.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