Spatio-Temporal Proteomics

Proteins are very dynamic, and their biological activity is influenced by regulated protein–protein interaction networks that respond to internal and external disturbances as well as temporal abundance variations. A plethora of novel analytical reagents and procedures enable highly granular studies of spatiotemporal protein environments while preserving high throughput and ease of analysis. In both health and disease, protein subcellular localization is carefully regulated and intimately connected to protein function. For a thorough understanding of cell biology, capturing the spatial proteome — that is, the localizations of proteins and their dynamics at the subcellular level — is crucial. The area is now mature for proteome-wide research of spatial cellular regulation, thanks to significant developments in microscopy, mass spectrometry, and machine learning tools for data interpretation. Assessing biological complexity, comprehending improved regulatory processes, and building protein complexes and networks all require spatiotemporal proteomics. Studying protein dynamics in space and time has the potential to reveal new information about how protein networks are disrupted during disease and aging, as well as open up new paths for therapeutic interventions, drug discovery, and biomarker development.