ArticleNucleic acids research2015
The ubiquitin ligase HERC3 attenuates NF-κB-dependent transcription independently of its enzymatic activity by delivering the RelA subunit for degradation.
Article in Nucleic acids research, 2015. 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, 28 citations in OpenAlex.
- HECT ubiquitin ligases as regulators of inflammatory signalling.Cell death and differentiation · 2026Review
- Integrative discovery and targeted proteomics elucidate the plasma exosomal landscape in thyroid disorders, with emphasis on papillary thyroid carcinoma complicating Hashimoto's thyroiditis.Frontiers in endocrinology · 2026Article
- SV2B Promotes the Progression of TFE3-Rearranged Renal Cell Carcinoma by Interacting with HERC2 to Impede the Degradation of NF-κB Subunits.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Epigenetic landscape of hormone-independent sexual dimorphism and characterization of canine XIST.Scientific reports · 2025Article
- How Can Molecules Induce Hemorrhoids? The Role of Genetics and Epigenetics in Hemorrhoidal Disease.International journal of molecular sciences · 2025Review
- Non-invasive urinary proteomic biomarkers for prognostic assessment in sepsis.Scientific reports · 2025Article
- Genomic Analysis of Sarda Sheep Raised at Diverse Temperatures Highlights Several Genes Involved in Adaptations to the Environment and Heat Stress Response.Animals : an open access journal from MDPI · 2024Article
- Fish HERC7: Phylogeny, Characterization, and Potential Implications for Antiviral Immunity in European Sea Bass.International journal of molecular sciences · 2024Article
- Oxypeucedanin hydrate alleviates rheumatoid arthritis by inhibiting the TLR4-MD2/NF-κB/MAPK signaling axis.Acta biochimica et biophysica Sinica · 2024Article
- E3 ubiquitin ligase Herc3 deficiency leads to accumulation of subretinal microglia and retinal neurodegeneration.Scientific reports · 2024Article
- HERC3 promotes YAP/TAZ stability and tumorigenesis independently of its ubiquitin ligase activity.The EMBO journal · 2023Article
- Epigenome-wide association study of serum folate in maternal peripheral blood leukocytes.Epigenomics · 2023Article
- Signaling pathways and therapeutic interventions in gastric cancer.Signal transduction and targeted therapy · 2022Review
- Investigation of the Anti-Inflammatory Activity of Fusaproliferin Analogues Guided by Transcriptome Analysis.Frontiers in pharmacology · 2022Article
- Quantitative and time-resolved miRNA pattern of early human T cell activation.Nucleic acids research · 2020Article
- Tau induces PSD95-neuronal NOS uncoupling and neurovascular dysfunction independent of neurodegeneration.Nature neuroscience · 2020Article
- How to Inactivate Human Ubiquitin E3 Ligases by Mutation.Frontiers in cell and developmental biology · 2020Review
- The Effect of Inflammation on the Formation of Thyroid Nodules.International journal of endocrinology · 2020Article
- KIAA0317 regulates pulmonary inflammation through SOCS2 degradation.JCI insight · 2019Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Activation of NF-κB-dependent transcription represents an important hallmark of inflammation. While the acute inflammatory response is per se beneficial, it can become deleterious if its spatial and temporal profile is not tightly controlled. Classically, NF-κB activity is limited by cytoplasmic retention of the NF-κB dimer through binding to inhibitory IκB proteins. However, increasing evidence suggests that NF-κB activity can also be efficiently contained by direct ubiquitination of NF-κB subunits. Here, we identify the HECT-domain ubiquitin ligase HERC3 as novel negative regulator of NF-κB activity. We find that HERC3 restricts NF-κB nuclear import and DNA binding without affecting IκBα degradation. Instead HERC3 indirectly binds to the NF-κB RelA subunit after liberation from IκBα inhibitor leading to its ubiquitination and protein destabilization. Remarkably, the regulation of RelA activity by HERC3 is independent of its inherent ubiquitin ligase activity. Rather, we show that HERC3 and RelA are part of a multi-protein complex containing the proteasome as well as the ubiquitin-like protein ubiquilin-1 (UBQLN1). We present evidence that HERC3 and UBQLN1 provide a link between NF-κB RelA and the 26S proteasome, thereby facilitating RelA protein degradation. Our findings establish HERC3 as novel candidate regulating the inflammatory response initiated by NF-κB.
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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.