ArticleNature communications2019
The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 19 citations in OpenAlex.
- Mapping Hsp104 interactions using cross-linking mass spectrometry.FEBS open bio · 2025Article
- Transforming an ATP-dependent enzyme into a dissipative, self-assembling system.Nature chemical biology · 2025Article
- Maintaining the Integral Membrane Proteome: Revisiting the Functional Repertoire of Integral Membrane Proteases.Chembiochem : a European journal of chemical biology · 2025Review
- Cryo-EM structure of AAA + ATPase thorase reveals novel helical filament formation.Computational and structural biotechnology journal · 2025Article
- Disulfide bond in SUN2 regulates dynamic remodeling of LINC complexes at the nuclear envelope.Life science alliance · 2023Article
- DYT-Frontiers in neuroscience · 2023Review
- Review
- Article
- Torsin and NEP1R1-CTDNEP1 phosphatase affect interphase nuclear pore complex insertion by lipid-dependent and lipid-independent mechanisms.The EMBO journal · 2021Article
- TorsinA folding and N-linked glycosylation are sensitive to redox homeostasis.Biochimica et biophysica acta. Molecular cell research · 2021Article
- AAA+ ATPases: structural insertions under the magnifying glass.Current opinion in structural biology · 2021Review
- Decreased mechanotransduction prevents nuclear collapse in aProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Lipid and protein dynamics that shape nuclear envelope identity.Molecular biology of the cell · 2020Review
- AAA+ proteins: converging mechanisms, diverging functions.Nature structural & molecular biology · 2020Article
- Article
- The Role of Torsin AAA+ Proteins in Preserving Nuclear Envelope Integrity and Safeguarding Against Disease.Biomolecules · 2020Review
- Resolving the TorsinA Oligomerization Conundrum: The Glycan Hypothesis.Frontiers in molecular biosciences · 2020Article
- An unbiased approach de-livers unexpected insight into torsin biology.The Journal of clinical investigation · 2019Article
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
TorsinA is an ER-resident AAA + ATPase, whose deletion of glutamate E303 results in the genetic neuromuscular disease primary dystonia. TorsinA is an unusual AAA + ATPase that needs an external activator. Also, it likely does not thread a peptide substrate through a narrow central channel, in contrast to its closest structural homologs. Here, we examined the oligomerization of TorsinA to get closer to a molecular understanding of its still enigmatic function. We observe TorsinA to form helical filaments, which we analyzed by cryo-electron microscopy using helical reconstruction. The 4.4 Å structure reveals long hollow tubes with a helical periodicity of 8.5 subunits per turn, and an inner channel of ~ 4 nm diameter. We further show that the protein is able to induce tubulation of membranes in vitro, an observation that may reflect an entirely new characteristic of AAA + ATPases. We discuss the implications of these observations for TorsinA function.
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