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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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“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]
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Metadata
- 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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