ArticleeLife2015
Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- The Ubiquitin Script: writing protein fates in chains.Essays in biochemistry · 2025Review
- Article
- Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Review
- Parkin-mediated ubiquitination inhibits BAK apoptotic activity by blocking its canonical hydrophobic groove.Communications biology · 2023Article
- DUBing Primary Tumors of the Central Nervous System: Regulatory Roles of Deubiquitinases.Biomolecules · 2023Review
- TheActa biochimica et biophysica Sinica · 2023Article
- Characterizing conformational ensembles of multi-domain proteins using anisotropic paramagnetic NMR restraints.Biophysical reviews · 2022Review
- Emerging Roles of Non-proteolytic Ubiquitination in Tumorigenesis.Frontiers in cell and developmental biology · 2022Review
- Recent Developments in Data-Assisted Modeling of Flexible Proteins.Frontiers in molecular biosciences · 2021Review
- The dynamics of linear polyubiquitin.Science advances · 2020Article
- GapR binds DNA through dynamic opening of its tetrameric interface.Nucleic acids research · 2020Article
- NMR Characterization of Conformational Interconversions of Lys48-Linked Ubiquitin Chains.International journal of molecular sciences · 2020Article
- Determination of Protein Structural Ensembles by Hybrid-Resolution SAXS Restrained Molecular Dynamics.Journal of chemical theory and computation · 2020Article
- Resolving the Complexity of Ubiquitin Networks.Frontiers in molecular biosciences · 2020Review
- Conformational and functional characterization of artificially conjugated non-canonical ubiquitin dimers.Scientific reports · 2019Article
- Requirement for p62 acetylation in the aggregation of ubiquitylated proteins under nutrient stress.Nature communications · 2019Article
- Diubiquitin-Based NMR Analysis: Interactions Between Lys6-Linked diUb and UBA Domain of UBXN1.Frontiers in chemistry · 2019Article
- Structural basis for the recognition of K48-linked Ub chain by proteasomal receptor Rpn13.Cell discovery · 2019Article
- Towards a molecular basis of ubiquitin signaling: A dual-scale simulation study of ubiquitin dimers.PLoS computational biology · 2018Article
- Extending chemical perturbations of the ubiquitin fitness landscape in a classroom setting reveals new constraints on sequence tolerance.Biology open · 2018Article
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Authors and funding
9 authors.
Funding
Abstract
A polyubiquitin comprises multiple covalently linked ubiquitins and recognizes myriad targets. Free or bound to ligands, polyubiquitins are found in different arrangements of ubiquitin subunits. To understand the structural basis for polyubiquitin quaternary plasticity and to explore the target recognition mechanism, we characterize the conformational space of Lys63-linked diubiquitin (K63-Ub2). Refining against inter-subunit paramagnetic NMR data, we show that free K63-Ub2 exists as a dynamic ensemble comprising multiple closed and open quaternary states. The quaternary dynamics enables K63-Ub2 to be specifically recognized in a variety of signaling pathways. When binding to a target protein, one of the preexisting quaternary states is selected and stabilized. A point mutation that shifts the equilibrium between the different states modulates the binding affinities towards K63-Ub2 ligands. This conformational selection mechanism at the quaternary level may be used by polyubiquitins of different lengths and linkages for target recognition.
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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.