邻近标记在蛋白质组学中的发展及应用

The complexity of life activities in humans are inseparable from protein-protein interactions (PPls). Most PPls are dynamic, especially by numerous transient post-translational modifications (PTM). Proximity labeling is a recently developed technique, which labels the potential binding proteins of a target protein based on proximity by biotin. It can be used in combination with mass spectrometry to detect weak and transient PPls in cellular processes. This paper reviews the development of different biotin-based proximity labeling methods. Starting from the biotin labeling method based on the fused substrate sequences, the principle of other labeling probes such as BirA^*, an engineered peroxidase (APEX), Bacillus subtilis (BASU) and APEX2 are discussed. Methods developed in the past few years such as antibody-targeted proximity labeling and split BioID are also introduced. The application and prospect of these methods in investigating PPls might inspire new researches in this field.