ArticleThe Journal of biological chemistry2009
Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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.
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.
Who cites it
61 citing papers in PubMed, 85 citations in OpenAlex.
- Whole genome sequencing reveals candidate causal genetic variants for spastic syndrome in Holstein cattle.Scientific reports · 2024Article
- LAP1 Interactome Profiling Provides New Insights into LAP1's Physiological Functions.International journal of molecular sciences · 2024Article
- 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 · 2024Article
- The clinical and genetic spectrum of autosomal-recessive TOR1A-related disorders.Brain : a journal of neurology · 2023Article
- Review
- Potential interactions between cerebellar dysfunction and sleep disturbances in dystonia.Dystonia (Lausanne, Switzerland) · 2022Article
- Impact of Nuclear Envelope Stress on Physiological and Pathological Processes in Central Nervous System.Neurochemical research · 2022Review
- p97/UBXD1 Generate Ubiquitylated Proteins That Are Sequestered into Nuclear Envelope Herniations in Torsin-Deficient Cells.International journal of molecular sciences · 2022Article
- Molecular Pathology of Laminopathies.Annual review of pathology · 2022Review
- Genetic evidence of aberrant striatal synaptic maturation and secretory pathway alteration in a dystonia mouse model.Dystonia (Lausanne, Switzerland) · 2022Article
- Review
- Structural Glycoprotein E2 of Classical Swine Fever Virus Critically Interacts with Host Protein Torsin-1A during the Virus Infectious Cycle.Journal of virology · 2021Article
- TorsinA restoration in a mouse model identifies a critical therapeutic window for DYT1 dystonia.The Journal of clinical investigation · 2021Article
- CNS critical periods: implications for dystonia and other neurodevelopmental disorders.JCI insight · 2021Review
- Decreased mechanotransduction prevents nuclear collapse in aProceedings of the National Academy of Sciences of the United States of America · 2020Article
- The abnormal firing of Purkinje cells in the knockin mouse model of DYT1 dystonia.Brain research bulletin · 2020Article
- Article
- The Role of Torsin AAA+ Proteins in Preserving Nuclear Envelope Integrity and Safeguarding Against Disease.Biomolecules · 2020Review
- The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn.Nature communications · 2019Article
- Expression of TorsinA in a heterologous yeast system reveals interactions with lumenal domains of LINC and nuclear pore complex components.Molecular biology of the cell · 2019Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Early onset (DYT1) torsion dystonia is a dominantly inherited movement disorder associated with a three-base pair (DeltaGAG) deletion that removes a glutamic acid residue from the protein torsinA. TorsinA is an essential AAA(+) (ATPases associated with a variety of cellular activities) ATPase found in the endoplasmic reticulum and nuclear envelope of higher eukaryotes, but what it does and how changes caused by the DeltaGAG deletion lead to dystonia are not known. Here, we asked how the DYT1 mutation affects association of torsinA with interacting proteins. Using immunoprecipitation and mass spectrometry, we first established that the related transmembrane proteins LULL1 and LAP1 are prominent binding partners for torsinA in U2OS cells. Comparative analysis demonstrates that these two proteins are targeted to the endoplasmic reticulum or nuclear envelope by their divergent N-terminal domains. Binding of torsinA to their C-terminal lumenal domains is stabilized when residues in any one of three motifs implicated in ATP hydrolysis (Walker B, sensor 1, and sensor 2) are mutated. Importantly, the DeltaGAG deletion does not stabilize this binding. Indeed, deleting the DeltaGAG encoded glutamic acid residue from any of the three ATP hydrolysis mutants destabilizes their association with LULL1 and LAP1C, suggesting a possible basis for loss of torsinA function. Impaired interaction of torsinA with LULL1 and/or LAP1 may thus contribute to the development of dystonia.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.