ArticleThe Journal of biological chemistry2013
Tripartite motif ligases catalyze polyubiquitin chain formation through a cooperative allosteric mechanism.
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 31 papers.
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Who cites it
31 citing papers in PubMed, 44 citations in OpenAlex.
- USP18 promotes nasopharyngeal carcinoma radioresistance via TRIM29 oligomerization and ubiquitination.Cell death and differentiation · 2026Article
- Review
- Trim39 regulates neuronal apoptosis by acting as a SUMO-targeted E3 ubiquitin-ligase for the transcription factor NFATc3.Cell death and differentiation · 2022Article
- Review
- Generation of the short TRIM32 isoform is regulated by Lys 247 acetylation and a PEST sequence.PloS one · 2021Article
- HDAC6 regulates antibody-dependent intracellular neutralization of viruses via deacetylation of TRIM21.The Journal of biological chemistry · 2020Article
- TRIM59 as a novel molecular biomarker to predict the prognosis of patients with NSCLC.Oncology letters · 2020Article
- Role of the E3 Ubiquitin Ligase TRIM4 in Predicting the Prognosis of Hepatocellular Carcinoma.Journal of Cancer · 2020Article
- The mammalian CTLH complex is an E3 ubiquitin ligase that targets its subunit muskelin for degradation.Scientific reports · 2019Article
- Article
- Enzymatic Logic of Ubiquitin Chain Assembly.Frontiers in physiology · 2019Review
- RING tetramerization is required for nuclear body biogenesis and PML sumoylation.Nature communications · 2018Article
- The mechanism of neural precursor cell expressed developmentally down-regulated 4-2 (Nedd4-2)/NEDD4L-catalyzed polyubiquitin chain assembly.The Journal of biological chemistry · 2017Article
- RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination.BMC biology · 2017Article
- Article
- Small-molecule inhibitors directly target CARD9 and mimic its protective variant in inflammatory bowel disease.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The TRIMendous Role of TRIMs in Virus-Host Interactions.Vaccines · 2017Review
- An Integrated Systems Biology Approach Identifies TRIM25 as a Key Determinant of Breast Cancer Metastasis.Cell reports · 2017Article
- Ubiquitin enzymes in the regulation of immune responses.Critical reviews in biochemistry and molecular biology · 2017Review
- Structural basis for the recognition and degradation of host TRIM proteins by Salmonella effector SopA.Nature communications · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ligation of polyubiquitin chains to proteins is a fundamental post-translational modification, often resulting in targeted degradation of conjugated proteins. Attachment of polyubiquitin chains requires the activities of an E1 activating enzyme, an E2 carrier protein, and an E3 ligase. The mechanism by which polyubiquitin chains are formed remains largely speculative, especially for RING-based ligases. The tripartite motif (TRIM) superfamily of ligases functions in many cellular processes including innate immunity, cellular localization, development and differentiation, signaling, and cancer progression. The present results show that TRIM ligases catalyze polyubiquitin chain formation in the absence of substrate, the rates of which can be used as a functional readout of enzyme function. Initial rate studies under biochemically defined conditions show that TRIM32 and TRIM25 are specific for the Ubc5 family of E2-conjugating proteins and, along with TRIM5α, exhibit cooperative kinetics with respect to Ubc5 concentration, with submicromolar [S]0.5 and Hill coefficients of 3-5, suggesting they possess multiple binding sites for their cognate E2-ubiquitin thioester. Mutation studies reveal a second, non-canonical binding site encompassing the C-terminal Ubc5α-helix. Polyubiquitin chain formation requires TRIM subunit oligomerization through the conserved coiled-coil domain, but can be partially replaced by fusing the catalytic domain to GST to promote dimerization. Other results suggest that TRIM32 assembles polyubiquitin chains as a Ubc5-linked thioester intermediate. These results represent the first detailed mechanistic study of TRIM ligase activity and provide a functional context for oligomerization observed in the superfamily.
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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.