Proximity Labeling Techniques: A Multi-Omics Toolbox

Proximity labeling techniques are emerging high-throughput methods for studying protein-protein, protein-RNA, and protein-DNA interactions with temporal and spatial precision. Proximity labeling methods take advantage of enzymes that can covalently label biomolecules with reactive substrates. These labeled biomolecules can be identified using mass spectrometry or next-generation sequencing. The main advantage of these methods is their ability to capture weak or transient interactions between biomolecules. Proximity labeling is indispensable for studying organelle interactomes. Additionally, it can be used to resolve spatial composition of macromolecular complexes. Many of these methods have only recently been introduced; nonetheless, they have already provided new and deep insights into the biological processes at the cellular, organ, and organism levels. In this paper, we review a broad range of proximity labeling techniques, their development, drawbacks and advantages, and implementations in recent studies.

Automated summary

Proximity labeling techniques provide a high-throughput approach to study protein-protein, protein-RNA, and protein-DNA interactions with precision. These methods utilize enzymes that can covalently label biomolecules, allowing for the identification of weak or transient interactions. The applications of proximity labeling extend to the analysis of organelle interactomes and spatial composition of macromolecular complexes.