Exogenous FGF-2 added to cells is internalized and part of it translocates
to the nucleus of the cells. To get a better understanding of the FGF-2-ind
uced signaling pathway, we looked for proteins associated with FGF-2 in the
cytoplasm of the target cells. We first used the GST-FGF-2 to isolate cyto
plasmic proteins complexes containing FGF-2 from S100 extract (supernatant
100,000g). Among the retrieved proteins, we focused our studies on RPS19, a
protein of the 40S small ribosomal subunit. We showed that FGF-2 interacts
directly with RPS19 in vitro. Second, we coimmunoprecipitated RPS19 and FG
F-2 from a S240 extract (240,000g supernatant) prepared from FGF-2-stimulat
ed cells and devoided of 40S ribosomal subunit. The result of these experim
ents suggest that a pool of free RPS19 exists in cells and that FGF-2 inter
acts in vivo with free RPS19. (C) 2001 Elsevier Science.