Translokin is an intracellular mediator of FGF-2 trafficking
Author: ["Carine Bossard","Henrik Laurell","Loïc Van den Berghe","Sylvain Meunier","Catherine Zanibellato","Hervé Prats"]
Publication: Nature Cell Biology
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Abstract
Basic fibroblast growth factor (bFGF or FGF-2) exerts its pleiotropic activities both as an exogenous and an intracellular factor. FGF-1 and FGF-2 are prototypes for this dual signalling, but the mechanisms of their intracellular actions remain unknown. Here we show that Translokin, a cytoplasmic protein of relative molecular mass 55,000 (Mr 55K), interacts specifically with the 18K form of FGF-2. Translokin is ubiquitously expressed and colocalizes with the microtubular network. As Translokin does not interact with FGF-1, we used a strategy based on FGF-1–FGF-2 chimaeras to map the interacting regions in FGF-2 and to generate Nb1a2, a non-interacting variant of FGF-2. Although most of the FGF-2 properties are preserved in Nb1a2, this variant is defective in intracellular translocation and in stimulating proliferation. The fusion of a nuclear localization signal to Nb1a2 restores its mitogenic activity and its nuclear association. Inhibiting Translokin expression by RNA interference reduces the translocation of FGF-2 without affecting the intracellular trafficking of FGF-1. Our data show that the nuclear association of internalized FGF-2 is essential for its mitogenic activity and that Translokin is important in this translocation pathway.
Cite this article
Bossard, C., Laurell, H., Van den Berghe, L. et al. Translokin is an intracellular mediator of FGF-2 trafficking. Nat Cell Biol 5, 433–439 (2003). https://doi.org/10.1038/ncb979
