Biotinylation-based proximity labelling proteomics: basics, applications and technical considerations

Recent advances in biotinylation-based proximity labelling (PL) have opened up new avenues for mapping the protein composition of cellular compartments and protein complexes in living cells at high spatiotemporal resolution. In particular, PL combined with mass spectrometry-based proteomics has been successfully applied to defining proteinprotein interactions, protein-nucleic acid interactions, (membraneless) organelle proteomes and secretomes in various systems ranging from cultured cells to whole animals. In this review, we first summarize the basics and recent biological applications of PL proteomics and then highlight recent developments in enrichment techniques for biotinylated proteins and peptides, focusing on the advantages of PL and technical considerations.

Automated summary

Recent advancements in biotinylation-based proximity labelling combined with mass spectrometry proteomics have been utilized for defining protein-protein interactions, protein-nucleic acid interactions, and organelle proteomes. With high spatiotemporal resolution, this technique is versatile for various systems.