TurboID-based proximity labeling accelerates discovery of neighboring proteins in plants

Identification of protein–protein interactions (PPIs) and protein compartmentalization is of great value for understanding cellular processes. Conventional affinity purification-mass spectrometry has low efficiency in detecting weak and/or transient PPIs. TurboID-based proximity labeling (PL) has emerged as an efficient tool that overcomes these weaknesses for identifying PPIs directly in the cellular environment. In PL, a bait is genetically fused to a biotin ligase (e.g., TurboID), which catalyzes the biotinylation of lysine residues of nearby proteins in living cells. Biotinylated neighboring proteins can be purified and identified using high-throughput mass spectrometry. TurboID-based solutions have been successfully applied in probing PPIs and proteomes of subcellular regions inside plant cells.