ArticleProceedings of the National Academy of Sciences of the United States of America2010
Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 92 citations in OpenAlex.
- VCP at the crossroads of UPS and autophagy in cancer.Genes & diseases · 2027Review
- Quantifying protein unfolding kinetics with a high-throughput microfluidic platform.Cell systems · 2026Article
- Structural proteomics reveals that misfolded nascent proteins expose buried lysines for ubiquitination and rapid proteasomal degradation.Cell reports · 2026Article
- The evolutionary dynamics between viral mimics and host proteins.Molecular systems biology · 2026Article
- Ubiquitination-Driven Reprogramming of Proteostasis in Metastasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Proteome-Wide Monitoring of Drug Action in Living Cells Using a Novel Label-Free Solvent-Based Shift Assay.Molecular & cellular proteomics : MCP · 2025Article
- Article
- The Thermodynamic Properties of Fat10ylated Proteins Are Regulated by the Fat10ylation Site.ACS omega · 2024Article
- Ubiquitin-Dependent and Independent Proteasomal Degradation in Host-Pathogen Interactions.Molecules (Basel, Switzerland) · 2023Review
- Post-translational Modifications in Brain Diseases: A Future for Biomarkers.Advances in experimental medicine and biology · 2022Article
- Mechanisms of substrate recognition by the 26S proteasome.Current opinion in structural biology · 2021Review
- In vivo modulation of ubiquitin chains by N-methylated non-proteinogenic cyclic peptides.RSC chemical biology · 2021Article
- Mechanistic basis for ubiquitin modulation of a protein energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Site-specific ubiquitination affects protein energetics and proteasomal degradation.Nature chemical biology · 2020Article
- Unraveling proteasome engagement.Nature chemical biology · 2020Article
- Ubiquitin receptors are required for substrate-mediated activation of the proteasome's unfolding ability.Scientific reports · 2019Article
- Melting Down Protein Stability: PAPS Synthase 2 in Patients and in a Cellular Environment.Frontiers in molecular biosciences · 2019Review
- Aim for the core: suitability of the ubiquitin-independent 20S proteasome as a drug target in neurodegeneration.Translational research : the journal of laboratory and clinical medicine · 2018Review
- Biological and Physicochemical Functions of Ubiquitylation Revealed by Synthetic Chemistry Approaches.International journal of molecular sciences · 2017Review
- Ubiquitylation Directly Induces Fold Destabilization of Proteins.Scientific reports · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein ubiquitination controls the cellular fate of numerous eukaryotic proteins. Despite its importance, many fundamental questions remain regarding its mechanism. One such question is how ubiquitination alters the biophysical properties of the modified protein and whether these alterations are significant in the cellular context. In this study, we investigate the effects of ubiquitination on the folding thermodynamics and mechanism of various substrates using computational tools and find that ubiquitination changes the thermal stability of modified proteins in a manner relevant to cellular processes. These changes depend on the substrate modification site and on the type of ubiquitination. Ubiquitination of the substrate Ubc7 at the residues that are modified in vivo prior to proteasomal degradation uniquely results in significant thermal destabilization and a local unwinding near the modification site, which indicates that ubiquitination possibly facilitates the unfolding process and improves substrate degradation efficiency. With respect to the substrate p19(4inkd), our results support a synergetic effect of ubiquitination and phosphorylation on the degradation process via enhanced thermal destabilization. Our study implies that, in addition to its known role as a recognition signal, the ubiquitin attachment may be directly involved in the cellular process it regulates by changing the biophysical properties of the substrate.
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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.