Evidence map›Paper›PMID 32204310›Full record

ReviewBiomolecules2020

The Role of Torsin AAA+ Proteins in Preserving Nuclear Envelope Integrity and Safeguarding Against Disease.

Anthony J Rampello, Sarah M Prophet, Christian Schlieker

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 11% of its field
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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. 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
  10. Article
  11. Nuclear envelope budding: Getting large macromolecular complexes out of the nucleus.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
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

3 authors at 1 institution in 1 country.

Anthony J RampelloDepartment of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520, USA.
Sarah M ProphetDepartment of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520, USA.
Christian SchliekerDepartment of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT 06520, USA.ORCID 0000-0002-1237-4267
Yale University · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
Structure-function analysis of Torsin ATPases in the context of the membraneR01GM114401 · NIGMS · YALE UNIVERSITY · PI SCHLIEKER, CHRISTIAN DIRK · 2016 to 2019
$1.3M
Defining the nuclear envelope-resident protein turnover machinery implicated in diseases affecting cholesterol metabolismR01GM126835 · NIGMS · YALE UNIVERSITY · PI SCHLIEKER, CHRISTIAN DIRK · 2018 to 2021
$1.3M
Foundation for the National Institutes of Health 5T32GM007223-44NIGMS NIH HHS R01 GM114401NIGMS NIH HHS R01 GM126835NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

Torsin ATPases are members of the AAA+ (ATPases associated with various cellular activities) superfamily of proteins, which participate in essential cellular processes. While AAA+ proteins are ubiquitously expressed and demonstrate distinct subcellular localizations, Torsins are the only AAA+ to reside within the nuclear envelope (NE) and endoplasmic reticulum (ER) network. Moreover, due to the absence of integral catalytic features, Torsins require the NE- and ER-specific regulatory cofactors, lamina-associated polypeptide 1 (LAP1) and luminal domain like LAP1 (LULL1), to efficiently trigger their atypical mode of ATP hydrolysis. Despite their implication in an ever-growing list of diverse processes, the specific contributions of Torsin/cofactor assemblies in maintaining normal cellular physiology remain largely enigmatic. Resolving gaps in the functional and mechanistic principles of Torsins and their cofactors are of considerable medical importance, as aberrant Torsin behavior is the principal cause of the movement disorder DYT1 early-onset dystonia. In this review, we examine recent findings regarding the phenotypic consequences of compromised Torsin and cofactor activities. In particular, we focus on the molecular features underlying NE defects and the contributions of Torsins to nuclear pore complex biogenesis, as well as the growing implications of Torsins in cellular lipid metabolism. Additionally, we discuss how understanding Torsins may facilitate the study of essential but poorly understood processes at the NE and ER, and aid in the development of therapeutic strategies for dystonia.

Indexed as

AnimalsDystoniaEndoplasmic ReticulumHSC70 Heat-Shock ProteinsHumansMolecular ChaperonesNuclear EnvelopeHSC70 Heat-Shock ProteinsHSPA8 protein, humanMolecular ChaperonesTOR1A protein, humanAAA+ ATPaselipinlow-density lipoprotein (VLDL)nuclear pore complex (NPC)TorsinA

Identifiers

PMID32204310
PMCPMC7175109
OpenAlexW3011067804

What OpenQuestion holds

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LicenceCC BY
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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.