Membrane-less and membrane-bound organelles provide sites for many crucial biological processes to take place within eukaryotic cells. Signalling and exchange of materials occurring at membrane contact sites (MCSs) among membrane-bound organelles are also vital for cell homeostasis. Proteomic mapping of molecular machineries within membrane-less organelles or MCSs are essential for the understanding all those events within such sites, as well as for the study of organelle interactions. However， the attempts to dissect molecular determinants in these sites using traditional biochemical techniques were far from fruitful. Recent advances in proximity labelling techniques provide an ideal solution for this challenge. Mostly by utilizing different type of biotin ligases which fused to target proteins， proteomes surrounding the target protein (within tens of nanometers) could be tagged (often with biotin or its derivatives). These covalently labelled proteins could then be enriched and identified with mass spectrometry.Here，we reviewed most recent advances in proximity labeling approaches， hoping to provide a general guide for researches focusing on proteomic mapping of molecular machineries within organelles or MCSs.