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08:58
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Published on: September 2, 2019
H2O2-free proximity proteomics for exploring dynamic protein complexes in living systems
Mi Ke1, Fuchao Liang1, Guangqin Wang2
1State Key Laboratory of Medical Proteomics and Shenzhen Key Laboratory of Functional Proteomics, Department of Chemistry and Research Center for Chemical Biology and Omics Analysis, College of Science and Guangming Advanced Research Institute, Southern University of Science and Technology, Shenzhen, China.
Nature Chemical Biology
|May 28, 2026
Summary
Researchers developed ROProx, a new proximity labeling method. This technique uses light to map protein interactions in living cells and mice without harmful chemicals, advancing biological research.
Area of Science:
- Biochemistry
- Molecular Biology
- Chemical Biology
Background:
- Dynamic protein complex assembly is crucial for biological regulation.
- Proximity labeling (PL) captures molecular events in cells but APEX2's H2O2 dependence limits its use in sensitive systems.
Purpose of the Study:
- Introduce ROProx, a novel photoreactive PL technology.
- Overcome limitations of H2O2-dependent labeling methods.
- Enable spatiotemporal mapping of protein interactions in living systems.
Main Methods:
- Leveraged the chemically evolved biotin-naphthylamine probe BN2 and APEX2 tyrosyl radicals.
- Utilized mild blue light irradiation for precise control.
- Applied ROProx in living cells and mice.
Main Results:
- ROProx labels dynamic cytosolic protein complexes within seconds.
- Achieved labeling with a 10 nm range, independent of H2O2.
- Successfully explored the phosphotyrosine-dependent GRB2 interactome in living mice.
Conclusions:
- ROProx offers a H2O2-free, light-controlled PL method for sensitive biological systems.
- Demonstrated ROProx's utility in live-cell and in vivo studies.
- ROProx expands possibilities for PL chemical evolution and applications.
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