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Nuclear fibroblast growth factor-2 interacts specifically with splicing factor SF3a66
Susanne Gringel1, Jeroen van Bergeijk, Kirsten Haastert
1Department of Neuroanatomy, Hannover Medical School, D-30625 Hannover, Germany.
Biological Chemistry
|January 18, 2005
Summary
Fibroblast growth factor 2 (FGF-2) acts intracellularly, binding to splicing factor SF3a66. This interaction suggests a novel nuclear function for FGF-2, impacting neurite outgrowth.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Fibroblast growth factor 2 (FGF-2) exhibits dual extracellular and intracellular functions.
- Intracellular FGF-2 isoforms, derived from alternative start codons, localize to distinct nuclear compartments.
- Understanding intracellular FGF-2 functions requires identifying its nuclear binding partners.
Purpose of the Study:
- To identify proteins interacting with intracellular Fibroblast growth factor 2 (FGF-2).
- To investigate the functional consequences of FGF-2 interactions within the nucleus.
- To explore a potential novel intranuclear role for FGF-2.
Main Methods:
- Yeast two-hybrid screening to identify FGF-2 interacting proteins.
- Pull-down assays to confirm protein-protein interactions.
- Functional neurite outgrowth assays to assess biological effects.
Main Results:
- The 66-kDa subunit of splicing factor 3a (SF3a66) was identified as an FGF-2 binding partner.
- FGF-2 interacted with both FGF-2(18) and FGF-2(23) isoforms, specifically with the C-terminus of SF3a66.
- SF3a66 demonstrated an enhancement of neurite outgrowth, similar to FGF-2(18).
Conclusions:
- FGF-2 interacts with SF3a66, a component of the splicing machinery.
- The interaction between FGF-2 and SF3a66 suggests a novel role in nuclear processes, potentially related to RNA splicing.
- The findings support a previously unrecognized intranuclear function for FGF-2, extending beyond its classical signaling pathways.