| First Author | Bossard C | Year | 2003 |
| Journal | Nat Cell Biol | Volume | 5 |
| Issue | 5 | Pages | 433-9 |
| PubMed ID | 12717444 | Mgi Jnum | J:83481 |
| Mgi Id | MGI:2662078 | Doi | 10.1038/ncb979 |
| Citation | Bossard C, et al. (2003) Translokin is an intracellular mediator of FGF-2 trafficking. Nat Cell Biol 5(5):433-9 |
| abstractText | 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 (M(r) 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. |
