In a post-genomic frame, the study of the dynamic process by which proteins interact in live cells will be pivotal to the determination of their functions. The spatio-temporal regulation of protein interactions is a key for understanding specific activation of signal transduction cascades. Spatial targeting of receptors to cell membrane domains and molecular associations and translocations, intracellular trafficking vary dynamically in a living cell. These are mechanisms that cells employ for rapid and accurate discrimination of signals.
The general interest of our group is to substitute the “hard-wired” diagrams of receptor –interactomes (i.e., a schematic representations of signaling pathways), with the real time dynamics of multi-protein complexes, as they assembly, translocate and disassembly in living cells, governing the mechanisms of cellular adhesion and migration.
Our studies take full advantage of the newest fluorescence based imaging techniques for single particle tracking, time resolved and fluorescence correlation spectroscopy. The flexibility and sensitivity of these approaches also allow their application to a large variety of in vitro ligand-protein interaction studies for the characterization of novel therapeutic targets and development of molecular-targeted new drugs.