Engineered allostery in light-regulated LOV-Turbo enables precise spatiotemporal control of proximity labeling in living cells
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Abstract
The incorporation of light-responsive domains into engineered proteins has enabled control of protein localization, interactions and function with light. We integrated optogenetic control into proximity labeling, a cornerstone technique for high-resolution proteomic mapping of organelles and interactomes in living cells. Through structure-guided screening and directed evolution, we installed the light-sensitive LOV domain into the proximity labeling enzyme TurboID to rapidly and reversibly control its labeling activity with low-power blue light. 'LOV-Turbo' works in multiple contexts and dramatically reduces background in biotin-rich environments such as neurons. We used LOV-Turbo for pulse-chase labeling to discover proteins that traffic between endoplasmic reticulum, nuclear and mitochondrial compartments under cellular stress. We also showed that instead of external light, LOV-Turbo can be activated by bioluminescence resonance energy transfer from luciferase, enabling interaction-dependent proximity labeling. Overall, LOV-Turbo increases the spatial and temporal precision of proximity labeling, expanding the scope of experimental questions that can be addressed with proximity labeling.
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Both biotin ligases and peroxidase can encounter background interference in cases of high endogenous biotin and H2O2 levels, respectively.
“Furthermore, both biotin ligases and peroxidase can encounter background interference in cases of high endogenous biotin and H2O2 levels, respectively25,26.”
From Spatiotemporally resolved mapping of extracellular proteomes via in vivo-compatible TyroID (2025) · cites this paper as [25]
The Abstract and Results (‘Applications enabled by LOV-Turbo’; page not provided) say that biotin already present in living organisms or culture media can cause TurboID background labeling before exogenous biotin is added. Our copy does not support the separate claim that high endogenous H2O2 causes background interference for peroxidases; searches for peroxidase and endogenous H2O2 did not find such a passage. (LLM, conf=0.88)
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BioLuminescent OptoGenetics in the choroid plexus: integrated opto- and chemogenetic control in vivo
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Evolving advances of proximity labeling in capturing biomolecular interactions
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Technologies to measure and modulate protein subcellular localization
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Emerging chemistries in proximity labeling
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Recent Advances in Proximity Labeling-Based Subcellular Proteomic Mapping
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Revealing protein trafficking by proximity labeling-based proteomics
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2D Nano‐Photosensitizer Facilitates Proximity Labeling for Living Cells Surfaceome Deciphering
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GlycoSS: A DNA Glycosignal Sieve for Deciphering Spatially Resolved EpCAM-Specific Glycoforms
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A brief guide to analyzing TurboID-based proximity labeling-mass spectrometry in plants
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AI-Assisted Native Proteomics: Delineating Ribosomal Protein Conformations Pre- and Post-Assembly
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TransitID maps translocated proteins en masse through tandem proximity labeling and enrichment
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- Authors
- Lee, S.-Y., Cheah, J. S., Zhao, B., Xu, C., Roh, H., Kim, C. K., Cho, K. F., Udeshi, N. D., Carr, S. A., & Ting, A. Y.
- Affiliations
- Stanford University (US)
- Broad Institute (US)
- University of California, Davis (US)
- Amgen (United States) (US)
- Chan Zuckerberg Biohub San Francisco (US)
- Corresponding author
- Ting, Alice Y.
- ORCID
- Venue
- Nature Methods
- Published
- 2023-05-15
- Volume
- 20
- Issue
- 6
- Pages
- 908-917
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- PMC
- PMC10539039
- OpenAlex
- W4376618234
- Cited by
- 118
- References
- 57
- Citations by year
- 2026: 32 · 2025: 45 · 2024: 29 · 2023: 12
- FWCI
- 17.08
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- Nature Methods (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- PubMed Central (submittedVersion)
- Funders
- U.S. Department of Health & Human Services | National Institutes of Health (RC2DK129964, R01-OD026223, T32GM007276)
- National Science Foundation (NeuroNex grant 2014862, GRFP DGE-1656518)
- National Research Foundation of Korea (NRF-2019R1A6A3A03033677)
- Burroughs Wellcome Fund (CASI 1019469)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- TurboID, LOV domain, optogenetics, allosteric regulation, spatiotemporal control, bioluminescence resonance energy transfer, pulse-chase labeling, protein trafficking, endoplasmic reticulum, mitochondria, nuclear proteins, cellular stress, protein-protein interaction
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