Evidence map›Paper›PMID 21785409›Full record

ArticleThe EMBO journal2011

Static retention of the lumenal monotopic membrane protein torsinA in the endoplasmic reticulum.

Abigail B Vander Heyden, Teresa V Naismith, Erik L Snapp, Phyllis I Hanson

Abstract readComparative Study
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. RANBP17 Overexpression Restores Nucleocytoplasmic Transport and Ameliorates Neurodevelopment in Induced DYT1 Dystonia Motor Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  5. DYT-Frontiers in neuroscience · 2023
    Review
  6. Article
  7. TorsinA folding and N-linked glycosylation are sensitive to redox homeostasis.Biochimica et biophysica acta. Molecular cell research · 2021
    Article
  8. The EViruses · 2021
    Article
  9. Disease Modeling with Human Neurons Reveals LMNB1 Dysregulation Underlying DYT1 Dystonia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. LINCing defective nuclear-cytoskeletal coupling and DYT1 dystonia.Cellular and molecular bioengineering · 2016
    Article
  18. Article
  19. Article
  20. Torsins: not your typical AAA+ ATPases.Critical reviews in biochemistry and molecular biology · 2015
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Abigail B Vander HeydenDepartment of Cell Biology and Physiology, Washington University School of Medicine, St Louis, MO, USA.
Teresa V Naismith
Erik L Snapp
Phyllis I Hanson

Funding

FUNCTIONAL ANALYSIS OF TORSIN AR01NS050717 · NINDS · WASHINGTON UNIVERSITY · PI HANSON, PHYLLIS I · 2004 to 2015
$2.4M
ER Chaperone Availability in Cells During Homeostasis and Misfolded Protein StresR01GM086530 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI SNAPP, ERIK L. · 2009 to 2010
$638k
Mechanism and regulation of LULL 1-directed NE enrichment of TorsinAF31NS065608 · NINDS · WASHINGTON UNIVERSITY · PI BUCHWALTER, ABIGAIL LYNN · 2010 to 2011
$48k
NIGMS NIH HHS R01 GM086530NINDS NIH HHS F31 NS065608NINDS NIH HHS R01 NS050717
6 · The paper itself

Abstract

TorsinA is a membrane-associated enzyme in the endoplasmic reticulum (ER) lumen that is mutated in DYT1 dystonia. How it remains in the ER has been unclear. We report that a hydrophobic N-terminal domain (NTD) directs static retention of torsinA within the ER by excluding it from ER exit sites, as has been previously reported for short transmembrane domains (TMDs). We show that despite the NTD's physicochemical similarity to TMDs, it does not traverse the membrane, defining torsinA as a lumenal monotopic membrane protein and requiring a new paradigm to explain retention. ER retention and membrane association are perturbed by a subset of nonconservative mutations to the NTD, suggesting that a helical structure with defined orientation in the membrane is required. TorsinA preferentially enriches in ER sheets, as might be expected for a lumenal monotopic membrane protein. We propose that the principle of membrane-based protein sorting extends to monotopic membrane proteins, and identify other proteins including the monotopic lumenal enzyme cyclooxygenase 1 (prostaglandin H synthase 1) that share this mechanism of retention with torsinA.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionCell MembraneCyclooxygenase 1Endoplasmic ReticulumGenes, ReporterHumansHydrophobic and Hydrophilic InteractionsMembrane ProteinsMolecular ChaperonesMolecular Sequence DataMutation, MissenseNuclear EnvelopeProtein Structure, SecondaryProtein Structure, TertiaryProtein TransportCyclooxygenase 1Membrane ProteinsMolecular ChaperonesPTGS1 protein, humanRecombinant Fusion ProteinsTOR1A protein, human

Identifiers

PMID21785409
PMCPMC3160655

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.