ArticleNature communications2014
Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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Who cites it
27 citing papers in PubMed, 51 citations in OpenAlex.
- SUMOylation enhances DNMT1 function to repress mega-intergenic RNAs and viral mimicry.Nature genetics · 2026Article
- Inhibition of coronaviral exoribonuclease activity by TRIM-mediated SUMOylation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Total Chemical Synthesis of RNF4 by Sequential Native Chemical Ligation: C-To-N Versus N-To-C Strategies.The Journal of organic chemistry · 2026Article
- Non-covalent SUMO interactions with ligases and effectors: SUMO-interacting motifs and beyond.Essays in biochemistry · 2025Review
- PML mutants from arsenic-resistant patients reveal SUMO1-TOPORS and SUMO2/3-RNF4 degradation pathways.The Journal of cell biology · 2025Article
- RNF4 mediated degradation of PDHA1 promotes colorectal cancer metabolism and metastasis.NPJ precision oncology · 2024Article
- Crosstalk between SUMOylation and other post-translational modifications in breast cancer.Cellular & molecular biology letters · 2024Review
- The physical and evolutionary energy landscapes of devolved protein sequences corresponding to pseudogenes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- NFATC2IP is a mediator of SUMO-dependent genome integrity.Genes & development · 2024Article
- Review
- The SUMO-NIP45 pathway processes toxic DNA catenanes to prevent mitotic failure.Nature structural & molecular biology · 2023Article
- The ubiquitin-dependent ATPase p97 removes cytotoxic trapped PARP1 from chromatin.Nature cell biology · 2022Article
- Uncover New Reactivity of Genetically Encoded Alkyl Bromide Non-Canonical Amino Acids.Frontiers in chemistry · 2022Article
- SUMO Interacting Motifs: Structure and Function.Cells · 2021Review
- SUMO-Targeted Ubiquitin Ligases and Their Functions in Maintaining Genome Stability.International journal of molecular sciences · 2021Review
- The SUMOylation pathway suppresses arbovirus replication in Aedes aegypti cells.PLoS pathogens · 2020Article
- Insights into the Microscopic Structure of RNF4-SIM-SUMO Complexes from MD Simulations.Biophysical journal · 2020Article
- Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer.Nature communications · 2020Article
- Dual functions of Aire CARD multimerization in the transcriptional regulation of T cell tolerance.Nature communications · 2020Article
- Arkadia/RNF111 is a SUMO-targeted ubiquitin ligase with preference for substrates marked with SUMO1-capped SUMO2/3 chain.Nature communications · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which targets substrates for proteasomal degradation. Here we use a segmental labelling approach combined with solution nuclear magnetic resonance (NMR) spectroscopy and biochemical characterization to reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer.
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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.