ArticleThe Journal of biological chemistry2016
Site-specific Proteolysis Mobilizes TorsinA from the Membrane of the Endoplasmic Reticulum (ER) in Response to ER Stress and B Cell Stimulation.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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Who cites it
20 citing papers in PubMed.
- TOR3A represses type I interferon production and limits viral clearance during respiratory syncytial virus infection.Emerging microbes & infections · 2026Article
- Elevated TOR1B expression predicts poor survival outcomes in patients with breast cancer.Genes & diseases · 2026Article
- Article
- Prognostic implications of TOR1B expression across cancer types: a focus on basal-like breast cancer and cellular adaptations to hypoxia.Journal of cancer research and clinical oncology · 2024Article
- Atypical nuclear envelope condensates linked to neurological disorders reveal nucleoporin-directed chaperone activities.Nature cell biology · 2022Article
- TorsinA folding and N-linked glycosylation are sensitive to redox homeostasis.Biochimica et biophysica acta. Molecular cell research · 2021Article
- Decreased mechanotransduction prevents nuclear collapse in aProceedings of the National Academy of Sciences of the United States of America · 2020Article
- 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
- The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn.Nature communications · 2019Article
- Combined loss of LAP1B and LAP1C results in an early onset multisystemic nuclear envelopathy.Nature communications · 2019Article
- Article
- CD19 Alterations Emerging after CD19-Directed Immunotherapy Cause Retention of the Misfolded Protein in the Endoplasmic Reticulum.Molecular and cellular biology · 2018Article
- Mutant torsinA in the heterozygous DYT1 state compromises HSV propagation in infected neurons and fibroblasts.Scientific reports · 2018Article
- Human TorsinA can function in the yeast cytosol as a molecular chaperone.The Biochemical journal · 2017Article
- Early-onset torsion dystonia: a novel high-throughput yeast genetic screen for factors modifying protein levels of torsinAΔE.Disease models & mechanisms · 2017Article
- TorsinA controls TAN line assembly and the retrograde flow of dorsal perinuclear actin cables during rearward nuclear movement.The Journal of cell biology · 2017Article
- Understanding the response to endurance exercise using a systems biology approach: combining blood metabolomics, transcriptomics and miRNomics in horses.BMC genomics · 2017Article
- Torsin ATPases: Harnessing Dynamic Instability for Function.Frontiers in molecular biosciences · 2017Article
- Dissecting Torsin/cofactor function at the nuclear envelope: a genetic study.Molecular biology of the cell · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Torsin ATPases are the only representatives of the AAA+ ATPase family that reside in the lumen of the endoplasmic reticulum (ER) and nuclear envelope. Two of these, TorsinA and TorsinB, are anchored to the ER membrane by virtue of an N-terminal hydrophobic domain. Here we demonstrate that the imposition of ER stress leads to a proteolytic cleavage event that selectively removes the hydrophobic domain from the AAA+ domain of TorsinA, which retains catalytic activity. Both the pharmacological inhibition profile and the identified cleavage site between two juxtaposed cysteine residues are distinct from those of presently known proteases, suggesting that a hitherto uncharacterized, membrane-associated protease accounts for TorsinA processing. This processing occurs not only in stress-exposed cell lines but also in primary cells from distinct organisms including stimulated B cells, indicating that Torsin conversion in response to physiologically relevant stimuli is an evolutionarily conserved process. By establishing 5-nitroisatin as a cell-permeable inhibitor for Torsin processing, we provide the methodological framework for interfering with Torsin processing in a wide range of primary cells without the need for genetic manipulation.
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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.