Spatio-temporal control of FGF2 recruitment and membrane translocation exerted by phosphoinositide and kinase switches. Fibroblast Growth Factor 2 (FGF2) is a mitogen involved in tumor-induced angiogenesis. FGF2 is secreted via an unconventional secretory pathway based upon direct translocation across the plasma membrane. This process is coordinated by both phosphoinositide and kinase switches controlling FGF2 oligomerization and membrane pore formation, the key intermediate in unconventional secretion of FGF2. This project aims at understanding the spatio-temporal coordination of this process in livings cells using advanced chemical biology tools and super-resolution, single molecule TIRF microscopy.