The scaffold protein FRS2 is overexpressed in medulloblastoma (MB) and correlates with aggressive tumor phenotype and poor prognosis. Studies regarding FRS2's interactome have been limited to the assembly of the well described canonical FGFR signalosome. Here, we explored the proteomic proximity of FRS2 in MB cells exposed to serum-free medium conditions, stimulation with bFGF or treatment with the FRS2 small molecule ligand C7. Towards this aim, we expressed APEX2 fused to FRS2 in UW228 cells and stimulated labeling activity by co-incubation with biotinphenol and hydrogen peroxide. In the control setup, we expressed a FRS2-mNeonGreen fusion without a peroxidase enzymatic function. After labling and streptavidin purification of biotinylated proteins, we performed mass spectrometry and quantified relative abundances compared to control conditions.