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

Biochem Biophys Res Commun. 2005 Dec 16;338(2):1248-55. doi: 10.1016/j.bbrc.2005.10.079. Epub 2005 Oct 24.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • COS Cells
  • Chlorocebus aethiops
  • Fibroblast Growth Factor 3 / chemistry*
  • Fibroblast Growth Factor 3 / metabolism*
  • Humans
  • Molecular Sequence Data
  • Protein Binding
  • Protein Interaction Mapping
  • Ribosomal Proteins / chemistry*
  • Ribosomal Proteins / metabolism*
  • Subcellular Fractions / metabolism*


  • Fibroblast Growth Factor 3
  • Ribosomal Proteins
  • ribosomal protein S2