ArticleThe Journal of biological chemistry2020
BioID screening of biotinylation sites using the avidin-like protein Tamavidin 2-REV identifies global interactors of stimulator of interferon genes (STING).
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 43 citations in OpenAlex.
- Integrated Network and Transcriptomic Analyses Identify a Candidate Ethanol-ADAM17 Molecular Axis Associated with Glioblastoma Progression.International journal of molecular sciences · 2026Article
- Evolutionary conservation analysis reveals a primordial function of STING as a regulator of lipid metabolism via FADS2.Nature communications · 2026Article
- DELLA proteins interact with HAC1 and control plant growth via transcriptional regulation of the growth repressor gene ERF2.The Plant cell · 2026Article
- STING signalling as a mediator between lipid metabolism and innate immunity.Nature reviews. Molecular cell biology · 2026Article
- STING is the scaffold protein for stress granule pre-condensation at the ER.Cell death and differentiation · 2026Article
- Spatial proteomics in precision medicine: technologies, bioinformatics, and translational applications.Precision clinical medicine · 2026Review
- Identification of MRVI1-interacting proteins by biotin-based proximity labelling reveals NPM-ALK-dependent interaction dynamics.Journal of biochemistry · 2025Article
- STING-mediated antiviral response: insights into MVA replication control in avian cells.Microbiology spectrum · 2025Article
- LAPTM5 exacerbates STING-mediated inflammation induced by LL-37 through stabilizing STING in rosacea.Communications biology · 2025Article
- In-cell proximity target validation methods for heterobifunctional molecules with CRBN- or VHL-binder using AirID.Communications biology · 2025Article
- An engineered redox-switchable streptavidin mutein enables the high-affinity capture and efficient elution of biotinylated ligands.Protein science : a publication of the Protein Society · 2025Article
- Overcoming Analytical Challenges in Proximity Labeling Proteomics.Journal of mass spectrometry : JMS · 2025Review
- Optimized Automated Workflow for BioID Improves Reproducibility and Identification of Protein-Protein Interactions.Journal of proteome research · 2024Article
- The Antiviral Activity of Interferon-Induced Transmembrane Proteins and Virus Evasion Strategies.Viruses · 2024Review
- Cytosolic DNA sensors in neurodegenerative diseases: from physiological defenders to pathological culprits.EMBO molecular medicine · 2024Review
- Workflow enhancement of TurboID-mediated proximity labeling for SPY signaling network mapping.bioRxiv : the preprint server for biology · 2024Article
- Proximity Labeling in Plants.Annual review of plant biology · 2023Review
- Dynamic Proximity Tagging in Living Plant Cells with Pupylation-Based Interaction Tagging.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Polo-Like Kinase 2 Plays an Essential Role in Cytoprotection against MG132-Induced Proteasome Inhibition via Phosphorylation of Serine 19 in HSPB5.International journal of molecular sciences · 2022Article
- A proximity biotinylation-based approach to identify protein-E3 ligase interactions induced by PROTACs and molecular glues.Nature communications · 2022Article
Corrections and comments
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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
Stimulator of interferon genes (STING) mediates cytosolic DNA-induced innate immune signaling via membrane trafficking. The global identification of proteins that spatiotemporally interact with STING will provide a better understanding of its trafficking mechanisms and of STING signaling pathways. Proximity-dependent biotin identification (BioID) is a powerful technology to identify physiologically relevant protein-protein interactions in living cells. However, biotinylated peptides are rarely detected in the conventional BioID method, which uses streptavidin beads to pull down biotinylated proteins, because the biotin-streptavidin interaction is too strong. As a result, only nonbiotinylated peptides are identified, which cannot be distinguished from peptides of nonspecifically pull-downed proteins. Here, we developed a simple method to efficiently and specifically enrich biotinylated peptides using Tamavidin 2-REV, an engineered avidin-like protein with reversible biotin-binding capability. Using RAW264.7 macrophages stably expressing TurboID-fused STING, we identified and quantified >4,000 biotinylated peptides of STING-proximal proteins. Various endoplasmic reticulum-associated proteins were biotinylated in unstimulated cells, and STING activation caused biotinylation of many proteins located in the Golgi and endosomes. These proteins included those known to interact with activated STING, such as TANK-binding kinase 1 (TBK1), several palmitoyl transferases, and p62/sequestosome 1 (SQSTM1). Furthermore, interferon-induced transmembrane protein 3 (IFITM3), an endolysosome-localized antiviral protein, bound to STING at the late activation stage. These dynamic interaction profiles will provide detailed insights into STING signaling; we propose that our approach using Tamavidin 2-REV would be useful for BioID-based and other biotinylation-based peptide identification methods.
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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.