ArticleScientific reports2017
A comprehensive platform for the analysis of ubiquitin-like protein modifications using in vivo biotinylation.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 67 citations in OpenAlex.
- A guide to mapping ubiquitin and ubiquitin-like E3 ligases to their substrates.The FEBS journal · 2026Review
- UFM1 at the endoplasmic reticulum: linking ER stress, ribosome quality control, and ER-phagy.Essays in biochemistry · 2025Review
- Quantum relaxometry for detecting biomolecular interactions with single NV centers.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- SUMO Antibody Validation.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Eg5 UFMylation promotes spindle organization during mitosis.Cell death & disease · 2024Article
- PIGB maintains nuclear lamina organization in skeletal muscle of Drosophila.The Journal of cell biology · 2024Article
- BioE3 identifies specific substrates of ubiquitin E3 ligases.Nature communications · 2023Article
- Review
- Mechanistic insights into the roles of the UFM1 E3 ligase complex in ufmylation and ribosome-associated protein quality control.Science advances · 2023Article
- SUMOylation of PDGF receptor α affects signaling via PLCγ and STAT3, and cell proliferation.BMC molecular and cell biology · 2023Article
- P-Rex1 is a novel substrate of the E3 ubiquitin ligase Malin associated with Lafora disease.Neurobiology of disease · 2023Article
- Neddylation is required for perinatal cardiac development through stimulation of metabolic maturation.Cell reports · 2023Article
- SUMO-ID: A Strategy for the Identification of SUMO-Dependent Proximal Interactors.Methods in molecular biology (Clifton, N.J.) · 2023Article
- A Computational Tool for Analysis of Mass Spectrometry Data of Ubiquitin-Enriched Samples.Methods in molecular biology (Clifton, N.J.) · 2023Article
- SUMO monoclonal antibodies vary in sensitivity, specificity, and ability to detect types of SUMO conjugate.Scientific reports · 2022Article
- Targeting Deubiquitinating Enzymes (DUBs) That Regulate Mitophagy via Direct or Indirect Interaction with Parkin.International journal of molecular sciences · 2022Review
- SUMOylation of Dorsal attenuates Toll/NF-κB signaling.Genetics · 2022Article
- The Next Frontier: Translational Development of Ubiquitination, SUMOylation, and NEDDylation in Cancer.International journal of molecular sciences · 2022Review
- Deubiquitinases in Neurodegeneration.Cells · 2022Review
- Maximizing Depth of PTM Coverage: Generating Robust MS Datasets for Computational Prediction Modeling.Methods in molecular biology (Clifton, N.J.) · 2022Review
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Authors and funding
13 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modification by ubiquitin and ubiquitin-like proteins (UbLs) is fundamental for maintaining protein homeostasis. Efficient isolation of UbL conjugates is hampered by multiple factors, including cost and specificity of reagents, removal of UbLs by proteases, distinguishing UbL conjugates from interactors, and low quantities of modified substrates. Here we describe bioUbLs, a comprehensive set of tools for studying modifications in Drosophila and mammals, based on multicistronic expression and in vivo biotinylation using the E. coli biotin protein ligase BirA. While the bioUbLs allow rapid validation of UbL conjugation for exogenous or endogenous proteins, the single vector approach can facilitate biotinylation of most proteins of interest. Purification under denaturing conditions inactivates deconjugating enzymes and stringent washes remove UbL interactors and non-specific background. We demonstrate the utility of the method in Drosophila cells and transgenic flies, identifying an extensive set of putative SUMOylated proteins in both cases. For mammalian cells, we show conjugation and localization for many different UbLs, with the identification of novel potential substrates for UFM1. Ease of use and the flexibility to modify existing vectors will make the bioUbL system a powerful complement to existing strategies for studying this important mode of protein regulation.
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