ArticleThe Journal of biological chemistry2015
Biophysical studies on interactions and assembly of full-size E3 ubiquitin ligase: suppressor of cytokine signaling 2 (SOCS2)-elongin BC-cullin 5-ring box protein 2 (RBX2).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 30 citations in OpenAlex.
- Native Mass Spectrometry Analysis of Cullin-RING Ubiquitin E3 Ligase Complexes in the Context of Targeted Protein Degradation.Analytical chemistry · 2026Article
- Interaction of CSN4 to DDB1 regulates its stability and function in DNA damage signaling.Cellular and molecular life sciences : CMLS · 2026Article
- Native Mass Spectrometry Analysis of Cullin RING Ubiquitin E3 Ligase Complexes in the Context of Targeted Protein Degradation.bioRxiv : the preprint server for biology · 2026Article
- Cul5: immune cell function and therapeutic potential.Frontiers in immunology · 2026Review
- The E3 ubiquitin ligase Cul5 regulates hematopoietic stem cell function for steady-state hematopoiesis in mice.The Journal of clinical investigation · 2025Article
- Structural insights into the ubiquitylation strategy of the oligomeric CRL2The EMBO journal · 2024Article
- Structure-based design of a phosphotyrosine-masked covalent ligand targeting the E3 ligase SOCS2.Nature communications · 2023Article
- Biophysical and functional study of CRL5Scientific reports · 2022Article
- Biochemical and Structural Insights into the Winged Helix Domain of P150, the Largest Subunit of the Chromatin Assembly Factor 1.International journal of molecular sciences · 2022Article
- SOCS proteins and their roles in the development of glioblastoma.Oncology letters · 2022Review
- NF-κB-activated SPRY4-IT1 promotes cancer cell metastasis by downregulating TCEB1 mRNA via Staufen1-mediated mRNA decay.Oncogene · 2021Article
- E3 Ligase Ligands for PROTACs: How They Were Found and How to Discover New Ones.SLAS discovery : advancing life sciences R & D · 2021Review
- Suppressor of Cytokine Signaling 2 Regulates Retinal Pigment Epithelium Metabolism by Enhancing Autophagy.Frontiers in neuroscience · 2021Article
- Assays and technologies for developing proteolysis targeting chimera degraders.Future medicinal chemistry · 2020Review
- Degronomics: Mapping the Interacting Peptidome of a Ubiquitin Ligase Using an Integrative Mass Spectrometry Strategy.Analytical chemistry · 2019Article
- Structural insights into substrate recognition by the SOCS2 E3 ubiquitin ligase.Nature communications · 2019Article
- Isatin-Schiff base-copper (II) complex induces cell death in p53-positive tumors.Cell death discovery · 2018Article
- Small Molecule Modulators of RING-Type E3 Ligases: MDM and Cullin Families as Targets.Frontiers in pharmacology · 2018Review
- Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex.Structure (London, England : 1993) · 2017Article
- [The Role of SOCS in the Development of Tumors].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2016Review
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
The multisubunit cullin RING E3 ubiquitin ligases (CRLs) target post-translationally modified substrates for ubiquitination and proteasomal degradation. The suppressors of cytokine signaling (SOCS) proteins play important roles in inflammatory processes, diabetes, and cancer and therefore represent attractive targets for therapeutic intervention. The SOCS proteins, among their other functions, serve as substrate receptors of CRL5 complexes. A member of the CRL family, SOCS2-EloBC-Cul5-Rbx2 (CRL5(SOCS2)), binds phosphorylated growth hormone receptor as its main substrate. Here, we demonstrate that the components of CRL5(SOCS2) can be specifically pulled from K562 human cell lysates using beads decorated with phosphorylated growth hormone receptor peptides. Subsequently, SOCS2-EloBC and full-length Cul5-Rbx2, recombinantly expressed in Escherichia coli and in Sf21 insect cells, respectively, were used to reconstitute neddylated and unneddylated CRL5(SOCS2) complexes in vitro. Finally, diverse biophysical methods were employed to study the assembly and interactions within the complexes. Unlike other E3 ligases, CRL5(SOCS2) was found to exist in a monomeric state as confirmed by size exclusion chromatography with inline multiangle static light scattering and native MS. Affinities of the protein-protein interactions within the multisubunit complex were measured by isothermal titration calorimetry. A structural model for full-size neddylated and unneddylated CRL5(SOCS2) complexes is supported by traveling wave ion mobility mass spectrometry data.
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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.