ArticleBiochemistry2013
Multimeric complexes among ankyrin-repeat and SOCS-box protein 9 (ASB9), ElonginBC, and Cullin 5: insights into the structure and assembly of ECS-type Cullin-RING E3 ubiquitin ligases.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- ASB9 promotes ubiquitin-mediated degradation of TNP2 to facilitate histone-to-protamine transition in humans and mice.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Mechanism of Histone Ubiquitylation by the ASB9-CUL5 Ubiquitin Ligase.Molecular & cellular proteomics : MCP · 2026Article
- ASB1 engages with ELOB to facilitate SQOR ubiquitination and HRedox biology · 2025Article
- Article
- Molecular insights into degron recognition by CRL5Nature communications · 2024Article
- Molecular evolution of Keap1 was essential for adaptation of vertebrates to terrestrial life.Science advances · 2023Article
- Biophysical and functional study of CRL5Scientific reports · 2022Article
- CUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation.Nature chemical biology · 2021Article
- Gonadotropin regulation of ankyrin-repeat and SOCS-box protein 9 (ASB9) in ovarian follicles and identification of binding partners.PloS one · 2019Article
- A Viral Protein Restricts Drosophila RNAi Immunity by Regulating Argonaute Activity and Stability.Cell host & microbe · 2018Article
- Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex.Structure (London, England : 1993) · 2017Article
- Working your SOCS off: The role of ASB10 and protein degradation pathways in glaucoma.Experimental eye research · 2017Review
- Model of the Ankyrin and SOCS Box Protein, ASB9, E3 Ligase Reveals a Mechanism for Dynamic Ubiquitin Transfer.Structure (London, England : 1993) · 2016Article
- The role of cullin 5-containing ubiquitin ligases.Cell division · 2016Review
- Targeting Cullin-RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation.The Biochemical journal · 2015Review
- How the ankyrin and SOCS box protein, ASB9, binds to creatine kinase.Biochemistry · 2015Article
- Insights into Cullin-RING E3 ubiquitin ligase recruitment: structure of the VHL-EloBC-Cul2 complex.Structure (London, England : 1993) · 2015Article
- 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).The Journal of biological chemistry · 2015Article
- Cullin E3 ligases and their rewiring by viral factors.Biomolecules · 2014Review
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4 authors.
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Abstract
Proteins of the ankyrin-repeat and SOCS-box (ASB) family act as the substrate-recognition subunits of ECS-type (ElonginBC-Cullin-SOCS-box) Cullin RING E3 ubiquitin ligase (CRL) complexes that catalyze the specific polyubiquitination of cellular proteins to target them for degradation by the proteasome. Therefore, ASB multimeric complexes are involved in numerous cell processes and pathways; however, their interactions, assembly, and biological roles remain poorly understood. To enhance our understanding of ASB CRL systems, we investigated the structure, affinity, and assembly of the quaternary multisubunit complex formed by ASB9, Elongin B, Elongin C (EloBC), and Cullin 5. Here, we describe the application of several biophysical techniques including differential scanning fluorimetry, isothermal titration calorimetry (ITC), nanoelectrospray ionization, and ion-mobility mass spectrometry (IM-MS) to provide structural and thermodynamic information for a quaternary ASB CRL complex. We find that ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain (Cul5NTD) but not to Cul2NTD. The structure of the monomeric ASB9-EloBC-Cul5NTD quaternary complex is revealed by molecular modeling and is consistent with IM-MS and temperature-dependent ITC data. This is the first experimental study to validate structural information for the assembly of the quaternary N-terminal region of an ASB CRL complex. The results suggest that ASB E3 ligase complexes function and assemble in an analogous manner to that of other CRL systems and provide a platform for further molecular investigation of this important protein family. The data reported here will also be of use for the future development of chemical probes to examine the biological function and modulation of other ECS-type CRL systems.
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