Fibroblast growth factor 3, a protein with a dual subcellular fate, is interacting with human ribosomal protein S2.

The secreted isoform of fibroblast growth factor 3 (FGF3) induces a mitogenic cell response, while the nuclear form inhibits cell proliferation. Recently, we identified a nucleolar FGF3-binding protein which is implicated in processing of pre-rRNA as a possible target of nuclear FGF3 signalling. Here, we report a second candidate protein ...
identified by a yeast two-hybrid screen for nuclear FGF3 action, ribosomal protein S2, rpS2. Recombinant rpS2 binds to in vitro translated FGF3 and to nuclear FGF3 extracted from transfected COS-1 cells. Characterization of the FGF3 binding domain of rpS2 showed that both the Arg-Gly-rich N-terminal region and a short carboxyl-terminal sequence of rpS2 are necessary for FGF3 binding. Mapping the S2 binding domains of FGF3 revealed that these domains are important for both NoBP and rpS2 interaction. Transient co-expression of rpS2 and nuclear FGF3 resulted in a reduced nucleolar localization of the FGF. These findings suggest that the nuclear form of FGF3 inhibits cell proliferation by interfering with ribosomal biogenesis.
Mesh Terms:
Amino Acid Sequence, Animals, Binding Sites, COS Cells, Cercopithecus aethiops, Fibroblast Growth Factor 3, Humans, Molecular Sequence Data, Protein Binding, Protein Interaction Mapping, Ribosomal Proteins, Subcellular Fractions
Biochem. Biophys. Res. Commun.
Date: Dec. 16, 2005
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