ArticleThe Journal of biological chemistry2013
The TREX1 C-terminal region controls cellular localization through ubiquitination.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- First case ofFrontiers in immunology · 2026Article
- Gigaxonin Potentiates Antiviral Innate Immune Responses by Targeting cGAS and TREX1.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Removal of TREX1 activity enhances CRISPR-Cas9-mediated homologous recombination.Nature biotechnology · 2025Article
- Inherited C-terminal TREX1 variants disrupt homology-directed repair to cause senescence and DNA damage phenotypes in Drosophila, mice, and humans.Nature communications · 2024Article
- Suppression ofiScience · 2023Article
- TREX1 cytosolic DNA degradation correlates with autoimmune disease and cancer immunity.Clinical and experimental immunology · 2023Article
- Distal Mutations in the β-Clamp of DNA Polymerase III* Disrupt DNA Orientation and Affect Exonuclease Activity.Journal of the American Chemical Society · 2023Article
- p53 engages the cGAS/STING cytosolic DNA sensing pathway for tumor suppression.Molecular cell · 2023Article
- Structural basis of human TREX1 DNA degradation and autoimmune disease.Nature communications · 2022Article
- Article
- TREX1 degrades the 3' end of the small DNA oligonucleotide products of nucleotide excision repair in human cells.Nucleic acids research · 2022Article
- cGAS phase separation inhibits TREX1-mediated DNA degradation and enhances cytosolic DNA sensing.Molecular cell · 2021Article
- The Role of Nucleases and Nucleic Acid Editing Enzymes in the Regulation of Self-Nucleic Acid Sensing.Frontiers in immunology · 2021Review
- TREX1 as a Novel Immunotherapeutic Target.Frontiers in immunology · 2021Article
- TREX1 - Apex predator of cytosolic DNA metabolism.DNA repair · 2020Article
- Changes to the TDP-43 and FUS Interactomes Induced by DNA Damage.Journal of proteome research · 2020Article
- Measuring TREX1 and TREX2 exonuclease activities.Methods in enzymology · 2019Article
- Structural basis for overhang excision and terminal unwinding of DNA duplexes by TREX1.PLoS biology · 2018Article
- Aicardi-Goutières syndrome protein TREX1 suppresses L1 and maintains genome integrity through exonuclease-independent ORF1p depletion.Nucleic acids research · 2017Article
- Immune Diseases Associated with TREX1 and STING Dysfunction.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2017Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
TREX1 is an autonomous 3'-exonuclease that degrades DNA to prevent inappropriate immune activation. The TREX1 protein is composed of 314 amino acids; the N-terminal 242 amino acids contain the catalytic domain, and the C-terminal region (CTR) localizes TREX1 to the cytosolic compartment. In this study, we show that TREX1 modification by ubiquitination is controlled by a highly conserved sequence in the CTR to affect cellular localization. Transfection of TREX1 deletion constructs into human cells demonstrated that this sequence is required for ubiquitination at multiple lysine residues through a "non-canonical" ubiquitin linkage. A proteomic approach identified ubiquilin 1 as a TREX1 CTR-interacting protein, and this interaction was verified in vitro and in vivo. Cotransfection studies indicated that ubiquilin 1 localizes TREX1 to cytosolic punctate structures dependent upon the TREX1 CTR and lysines within the TREX1 catalytic core. Several TREX1 mutants linked to the autoimmune diseases Aicardi-Goutières syndrome and systemic lupus erythematosus that exhibit full catalytic function were tested for altered ubiquitin modification and cellular localization. Our data show that these catalytically competent disease-causing TREX1 mutants exhibit differential levels of ubiquitination relative to WT TREX1, suggesting a novel mechanism of dysfunction. Furthermore, these differentially ubiquitinated disease-causing mutants also exhibit altered ubiquilin 1 co-localization. Thus, TREX1 post-translational modification indicates an additional mechanism by which mutations disrupt TREX1 biology, leading to human autoimmune disease.
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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.