ArticleCommunications biology2024
Super-resolution proximity labeling with enhanced direct identification of biotinylation sites.
Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- In vivo labeling-based proteomic analysis of early follicle oocytes and cisplatin-induced alterations in mice.Nature communications · 2026Article
- Spatiotemporally Resolved Protein Tagging for Dynamic and Tissue-Specific Secretome Profiling In Vivo.Angewandte Chemie (International ed. in English) · 2026Article
- Serpina1e mediates the exercise-induced enhancement of hippocampal memory in male mice.Nature communications · 2026Article
- Chemical biology approaches to study and target circadian clocks and their components.FEBS letters · 2026Review
- Proximity labeling unveils potential roles of the Miro2-CISD1 network in mitochondrial dynamics and neuronal differentiation.Communications biology · 2026Article
- Proximity labeling in neuroscience: decoding molecular landscapes for precision neurology.Translational neurodegeneration · 2026Review
- Integrating endogenous TurboID and data-independent acquisition mass spectrometry for in vivo proximity labeling.The EMBO journal · 2026Article
- Intracristal space proteome mapping using super-resolution proximity labeling with isotope-coded probes.Nature communications · 2025Article
- Adaptation of the Protocol for the Isolation of Biotinylated Protein Complexes forInternational journal of molecular sciences · 2025Article
- Bridging molecular and cellular neuroscience with proximity labeling technologies.Experimental & molecular medicine · 2025Review
- A Straightforward Interpretation of Proximity Labeling through Direct Biotinylation Analysis.ACS omega · 2025Article
- Review
- Review
- Precision proteomics with TurboID: mapping the suborganelle landscape.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2024Review
- Mass Spectrometry-Based Proteomics Technologies to Define Endogenous Protein-Protein Interactions and Their Applications to Cancer and Viral Infectious Diseases.Mass spectrometry reviewsReview
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Authors and funding
7 authors.
Funding
Abstract
Promiscuous labeling enzymes, such as APEX2 or TurboID, are commonly used in in situ biotinylation studies of subcellular proteomes or protein-protein interactions. Although the conventional approach of enriching biotinylated proteins is widely implemented, in-depth identification of specific biotinylation sites remains challenging, and current approaches are technically demanding with low yields. A novel method to systematically identify specific biotinylation sites for LC-MS analysis followed by proximity labeling showed excellent performance compared with that of related approaches in terms of identification depth with high enrichment power. The systematic identification of biotinylation sites enabled a simpler and more efficient experimental design to identify subcellular localized proteins within membranous organelles. Applying this method to the processing body (PB), a non-membranous organelle, successfully allowed unbiased identification of PB core proteins, including novel candidates. We anticipate that our newly developed method will replace the conventional method for identifying biotinylated proteins labeled by promiscuous labeling enzymes.
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