ArticleProceedings of the National Academy of Sciences of the United States of America2013
Conformational dynamics control ubiquitin-deubiquitinase interactions and influence in vivo signaling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 56 citations in OpenAlex.
- Pex30-dependent membrane contact sites maintain ER lipid homeostasis.The Journal of cell biology · 2025Article
- Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Review
- Ubiquitin Engineering for Interrogating the Ubiquitin-Proteasome System and Novel Therapeutic Strategies.Cells · 2023Review
- On the Study of Deubiquitinases: Using the Right Tools for the Job.Biomolecules · 2022Review
- Kinetic Constraints in the Specific Interaction between Phosphorylated Ubiquitin and Proteasomal Shuttle Factors.Biomolecules · 2021Article
- Targeting the Ubiquitin Signaling Cascade in Tumor Microenvironment for Cancer Therapy.International journal of molecular sciences · 2021Review
- Understanding the Binding Transition State After the Conformational Selection Step: The Second Half of the Molecular Recognition Process Between NS1 of the 1918 Influenza Virus and Host p85β.Frontiers in molecular biosciences · 2021Article
- The Role of Conformational Dynamics in the Recognition and Regulation of Ubiquitination.Molecules (Basel, Switzerland) · 2020Review
- Could confounding the allosteric communication of biotic machinery be an alternative path to antibiotics?Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Modulating protein-protein interaction networks in protein homeostasis.Current opinion in chemical biology · 2019Review
- Origin of conformational dynamics in a globular protein.Communications biology · 2019Article
- Conformational Dynamics Modulate Activation of the Ubiquitin Conjugating Enzyme Ube2g2.ACS omega · 2017Article
- Dynamic Modulation of Binding Affinity as a Mechanism for Regulating Interferon Signaling.Journal of molecular biology · 2017Article
- USP14 de-ubiquitinates vimentin and miR-320a modulates USP14 and vimentin to contribute to malignancy in gastric cancer cells.Oncotarget · 2017Article
- A Slow Conformational Switch in the BMAL1 Transactivation Domain Modulates Circadian Rhythms.Molecular cell · 2017Article
- Flexibility and Design: Conformational Heterogeneity along the Evolutionary Trajectory of a Redesigned Ubiquitin.Structure (London, England : 1993) · 2017Article
- Structural and functional characterization of a ubiquitin variant engineered for tight and specific binding to an alpha-helical ubiquitin interacting motif.Protein science : a publication of the Protein Society · 2017Article
- Specific targeting of the deubiquitinase and E3 ligase families with engineered ubiquitin variants.Bioengineering & translational medicine · 2017Review
- MicroRNA-17 Suppresses TNF-α Signaling by Interfering with TRAF2 and cIAP2 Association in Rheumatoid Arthritis Synovial Fibroblasts.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- Divergence in Ubiquitin Interaction and Catalysis among the Ubiquitin-Specific Protease Family Deubiquitinating Enzymes.Biochemistry · 2016Article
Corrections and comments
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Authors and funding
14 authors at 1 institution.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitin is a highly conserved eukaryotic protein that interacts with a diverse set of partners to act as a cellular signaling hub. Ubiquitin's conformational flexibility has been postulated to underlie its multifaceted recognition. Here we use computational and library-based means to interrogate core mutations that modulate the conformational dynamics of human ubiquitin. These ubiquitin variants exhibit increased affinity for the USP14 deubiquitinase, with concomitantly reduced affinity for other deubiquitinases. Strikingly, the kinetics of conformational motion are dramatically slowed in these variants without a detectable change in either the ground state fold or excited state population. These variants can be ligated into substrate-linked chains in vitro and in vivo but cannot solely support growth in eukaryotic cells. Proteomic analyses reveal nearly identical interaction profiles between WT ubiquitin and the variants but identify a small subset of altered interactions. Taken together, these results show that conformational dynamics are critical for ubiquitin-deubiquitinase interactions and imply that the fine tuning of motion has played a key role in the evolution of ubiquitin as a signaling hub.
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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.