Synthesis of proteins or translation, is one of the most energy-expensive processes in cells and hence, during stressful conditions cells have evolved various pathways to down-regulate this process. In this talk, I will discuss our findings about one particular strategy adopted by some messenger RNA molecules, which bypasses a key stress-induced regulatory step of translation initiation and allows the synthesis of a specific sub-set of proteins via an alternate pathway that promote many pathological conditions, including tumor development. 

Fibroblast growth factor (FGF) signaling is primarily regulated via the binding specificity between a given FGF ligand and its cognate receptor(s). In an effort to elucidate the structural basis whereby the entire FGF7 subfamily attains its tight binding specificity for the "b" isoform of FGF receptor 2 (FGFR2b), we recently solved the crystal structure of the FGF3-FGFR2b complex. The crystal structure highlights a novel mode of FGFR-binding specificity unique to the FGF7 subfamily, and provides a molecular rationale for why FGF7 subfamily ligands differ quantitatively in their capacities to activate FGFR2b. We propose that these differences may account for the non-overlapping roles each of the FGF7 subfamily members play in mammalian biology.