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A more recent version of this article appeared on September 7, 2007
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M611234200v1
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Papers In Press, published online ahead of print July 6, 2007
J. Biol. Chem, 10.1074/jbc.M611234200
Submitted on December 7, 2006
Revised on June 29, 2007
Accepted on July 6, 2007

A nuclear export sequence located on a beta -strand in fibroblast growth factor-1

Trine Nilsen, Ken Roger Rosendal, Vigdis Sørensen, Jørgen Wesche, Sjur Olsnes, and Antoni Wiedlocha

Deartment of Biochemistry, Rikshospitalet-Radiumhospitalet Medical Centre, Oslo 0310

Corresponding Author: antoni.wiedlocha{at}rr-research.no

Receptor-bound and endocytosed fibroblast growth factor-1 (FGF-1) is able to cross the vesicle membrane and translocate to cytosol and nucleus. This suggests an intracellular role of FGF-1, which also signals by activating transmembrane FGF receptors. Phosphorylation of internalised FGF-1 by nuclear protein kinase C delta (PKC) induces rapid export from the nuclei by a Leptomycin B (LMB) sensitive pathway. In the present work we have searched for and identified a Leu-rich nuclear export sequence (NES) at the C-terminus of FGF-1 required for its nuclear export and able to confer nuclear export activity to a reporter protein in an in vivo system. Mutants where hydrophobic amino acids within the NES were exchanged for alanine exhibited reduced or abolished nuclear export. As demonstrated in co-immunoprecipitation experiments, a complex containing FGF-1, Exportin-1 and its co-factor Ran-GTP, was formed in vitro. Formation of this complex in vivo was demonstrated by a peroxisomal targeting assay. Formation of the FGF-1-Exportin-1-Ran-GTP complex in vitro as well as nuclear export of FGF-1 in vivo was dependent on phosphorylation of FGF-1 and it was abolished by LMB. The FGF-1 NES was found to be situated along a beta-strand, which has not been reported before as NESs usually are alpha-helical.


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