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Journal of Cell Science, Vol 113, Issue 10 1827-1838, Copyright © 2000 by Company of Biologists
JOURNAL ARTICLES |
O Klingenberg, A Wiedlocha, A Rapak, D Khnykin, L Citores and S Olsnes
Institute for Cancer Research, The Norwegian Radium Hospital, Montebello, Norway.
The ability of COS cells to bind and internalise acidic fibroblast growth factor (aFGF) was studied after transient transfection of the cells with wild-type and mutated fibroblast growth factor receptor 4. In one case the tyrosine kinase of the receptor was inactivated by a point mutation in the active site, whereas in other cases parts of the receptor were deleted to remove various parts of the cytoplasmic domain. In all cases the receptors were expressed at the cell surface at a high level and the cells bound labelled growth factor efficiently and internalised it by endocytosis. Translocation of externally added aFGF across cellular membranes to reach the cytosol and nucleus was measured as transport of labelled growth factor to the nuclear fraction obtained by centrifugation, by farnesylation of growth factor modified to carry a CAAX motif, and by phosphorylation of the growth factor at a site specific for protein kinase C. Whereas both full-length receptors (with and without an active kinase domain) facilitated translocation of the growth factor to the cytosol and nucleus, as assessed by these methods, the mutants of the receptor where the C terminus was deleted, were unable to do so. In contrast, a receptor containing only the 57 most C-terminal amino acids of the cytoplasmic domain in addition to the juxtamembrane, transmembrane and extracellular domains, was in fact able to mediate translocation of aFGF to the cytosol. These data indicate that information contained in the C terminus of the receptor is required for translocation.
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  E. M. Haugsten, J. Malecki, S. M. S. Bjorklund, S. Olsnes, and J. Wesche Ubiquitination of Fibroblast Growth Factor Receptor 1 Is Required for Its Intracellular Sorting but Not for Its Endocytosis Mol. Biol. Cell, August 1, 2008; 19(8): 3390 - 3403. [Abstract] [Full Text] [PDF]
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 V. Sorensen, Y. Zhen, M. Zakrzewska, E. M. Haugsten, S. Walchli, T. Nilsen, S. Olsnes, and A. Wiedlocha Phosphorylation of Fibroblast Growth Factor (FGF) Receptor 1 at Ser777 by p38 Mitogen-Activated Protein Kinase Regulates Translocation of Exogenous FGF1 to the Cytosol and Nucleus Mol. Cell. Biol., June 15, 2008; 28(12): 4129 - 4141. [Abstract] [Full Text] [PDF]
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 T. Nilsen, K. R. Rosendal, V. Sorensen, J. Wesche, S. Olsnes, and A. Wiedlocha A Nuclear Export Sequence Located on a beta-Strand in Fibroblast Growth Factor-1 J. Biol. Chem., September 7, 2007; 282(36): 26245 - 26256. [Abstract] [Full Text] [PDF]
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 V. Sorensen, A. Wiedlocha, E. M. Haugsten, D. Khnykin, J. Wesche, and S. Olsnes Different abilities of the four FGFRs to mediate FGF-1 translocation are linked to differences in the receptor C-terminal tail J. Cell Sci., October 15, 2006; 119(20): 4332 - 4341. [Abstract] [Full Text] [PDF]
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E. M. Haugsten, V. Sorensen, A. Brech, S. Olsnes, and J. Wesche Different intracellular trafficking of FGF1 endocytosed by the four homologous FGF receptors J. Cell Sci., September 1, 2005; 118(17): 3869 - 3881. [Abstract] [Full Text] [PDF]
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V. Sorensen, A. Brech, D. Khnykin, E. Kolpakova, L. Citores, and S. Olsnes Deletion mutant of FGFR4 induces onion-like membrane structures in the nucleus J. Cell Sci., May 1, 2004; 117(9): 1807 - 1819. [Abstract] [Full Text] [PDF]
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 S. Olsnes, O. Klingenberg, and A. Wiedlocha Transport of Exogenous Growth Factors and Cytokines to the Cytosol and to the Nucleus Physiol Rev, January 1, 2003; 83(1): 163 - 182. [Abstract] [Full Text] [PDF]
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L Citores, D Khnykin, V Sorensen, J Wesche, O Klingenberg, A Wiedlocha, and S Olsnes Modulation of intracellular transport of acidic fibroblast growth factor by mutations in the cytoplasmic receptor domain J. Cell Sci., January 5, 2001; 114(9): 1677 - 1689. [Abstract] [PDF]
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