ArticleThe Biochemical journal2014
Multivalent interactions of the SUMO-interaction motifs in RING finger protein 4 determine the specificity for chains of the SUMO.
Article in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Role of Nuclear SUMO-Targeted Ubiquitin Ligase Uls2 (Slx5-Slx8) in Quality Control of Cytosolic Proteins.Biomolecules · 2026Article
- Recruitment of Mre11 to recombination sites during meiosis.Nature communications · 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
- Cysteine-reactive covalent chloro-N-acetamide ligands induce ferroptosis mediated cell death.EMBO reports · 2025Article
- Review
- RNF4 and USP7 cooperate in ubiquitin-regulated steps of DNA replication.Open biology · 2023Article
- A Photo-Crosslinking Approach to Identify Class II SUMO-1 Binders.Frontiers in chemistry · 2022Article
- Deorphanizing Caspase-3 and Caspase-9 Substrates In and Out of Apoptosis with Deep Substrate Profiling.ACS chemical biology · 2021Article
- Ring finger protein 213 assembles into a sensor for ISGylated proteins with antimicrobial activity.Nature communications · 2021Article
- SUMO-Targeted Ubiquitin Ligases and Their Functions in Maintaining Genome Stability.International journal of molecular sciences · 2021Review
- Insights into the Microscopic Structure of RNF4-SIM-SUMO Complexes from MD Simulations.Biophysical journal · 2020Article
- Wss1 homolog from Candida albicans and its role in DNA-protein crosslink tolerance.Molecular microbiology · 2020Article
- Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer.Nature communications · 2020Article
- Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility.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
- Review
- Quantitative SUMO proteomics reveals the modulation of several PML nuclear body associated proteins and an anti-senescence function of UBC9.Scientific reports · 2018Article
- The post-translational modification, SUMOylation, and cancer (Review).International journal of oncology · 2018Review
- Ubiquitin-like Protein Conjugation: Structures, Chemistry, and Mechanism.Chemical reviews · 2018Review
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNF4 (RING finger protein 4) is a STUbL [SUMO (small ubiquitin-related modifier)-targeted ubiquitin ligase] controlling PML (promyelocytic leukaemia) nuclear bodies, DNA double strand break repair and other nuclear functions. In the present paper, we describe that the sequence and spacing of the SIMs (SUMO-interaction motifs) in RNF4 regulate the avidity-driven recognition of substrate proteins carrying SUMO chains of variable length.
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