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

Abstract:

: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.

authors

Antoine M,Reimers K,Wirz W,Gressner AM,Müller R,Kiefer P

doi

10.1016/j.bbrc.2005.10.079

subject

Has Abstract

pub_date

2005-12-16 00:00:00

pages

1248-55

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)02338-7

journal_volume

338

pub_type

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