ArticleMethods in molecular biology (Clifton, N.J.)2025
On-Demand Proximity Labeling Using Light-Activated BioID.
Article in Methods in molecular biology (Clifton, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Membrane proteins play essential roles in the formation and maintenance of tissues. However, mapping the interactomes of membrane proteins is challenging with traditional proteomic methods. A common technique for investigating protein-protein interactions (PPIs) uses genetically encoded enzymes, such as TurboID, to label nearby proteins with biotin tags for subsequent detection. However, TurboID-mediated biotinylation cannot be switched on or off on demand, which results in high off-target or background labeling. To address this limitation and map membrane PPIs with high spatial and temporal resolution, we developed a novel light-activated proximity labeling technology: Light-Activated BioID (LAB). This innovative tool combines the two halves of the split-TurboID proximity labeling enzyme with photodimeric proteins CRY2 and CIB1, creating a user-controlled proximity biotinylation system for precise mapping of PPIs of membrane-bound proteins. In this work, we present our methods for developing, testing, and utilizing LAB to map PPIs.
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