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Volumn 134, Issue 2, 1996, Pages 529-536

Nuclear translocation of fibroblast growth factor (FGF) receptors in response to FGF-2

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN; CELL SURFACE PROTEIN; FIBROBLAST GROWTH FACTOR 1; FIBROBLAST GROWTH FACTOR 2; FIBROBLAST GROWTH FACTOR RECEPTOR;

EID: 0029954235     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.134.2.529     Document Type: Article
Times cited : (202)

References (44)
  • 1
    • 0001112290 scopus 로고
    • Fibroblast growth factors
    • M.B. Sporn and A.B. Roberts, editors. Verlag, Berlin
    • Baird, A., and P. Bohlen. 1990. Fibroblast growth factors. In Peptide Growth Factors and Their Receptors. M.B. Sporn and A.B. Roberts, editors. Verlag, Berlin. 369-418.
    • (1990) Peptide Growth Factors and Their Receptors , pp. 369-418
    • Baird, A.1    Bohlen, P.2
  • 3
    • 0024339705 scopus 로고
    • The heparin-binding (fibroblast) growth factor family of proteins
    • Burgess, W.H., and T. Maciag. 1989. The heparin-binding (fibroblast) growth factor family of proteins. Annu. Rev. Biochem. 58:575-606.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 575-606
    • Burgess, W.H.1    Maciag, T.2
  • 4
    • 0023276106 scopus 로고
    • Biotinylation: An alternative to radioiodination for the identification of cell surface antigens in immunoprecipitates
    • Cole, S.R., L.K. Ashman, and P.L. Ey. 1987. Biotinylation: an alternative to radioiodination for the identification of cell surface antigens in immunoprecipitates. Mol. Immunol. 24:699-705.
    • (1987) Mol. Immunol. , vol.24 , pp. 699-705
    • Cole, S.R.1    Ashman, L.K.2    Ey, P.L.3
  • 5
    • 0025181895 scopus 로고
    • IL-1 and its receptor are translocated to the nucleus
    • Curtis, H.M., M.B. Widmer, P. DeRoos, and E.E. Qwarnstrom. 1990. IL-1 and its receptor are translocated to the nucleus. J. Immunol. 144:1295-1303.
    • (1990) J. Immunol. , vol.144 , pp. 1295-1303
    • Curtis, H.M.1    Widmer, M.B.2    DeRoos, P.3    Qwarnstrom, E.E.4
  • 6
    • 0025949412 scopus 로고
    • Nuclear targeting sequences - A consensus?
    • Dingwall, C., and R.A. Laskey, 1991. Nuclear targeting sequences - a consensus? Trends Biochem. Sci. 16:478-481.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 7
    • 0025372116 scopus 로고
    • Progressive changes in the protein composition of the nuclear matrix during rat osteoblast differentiation
    • Dworetsky, S.I., E.G. Fey, S. Penman, J.B. Lian, J.L. Stein, and G.S. Stein. 1990. Progressive changes in the protein composition of the nuclear matrix during rat osteoblast differentiation. Proc. Natl. Acad. Sci. USA. 87:4605-4609.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4605-4609
    • Dworetsky, S.I.1    Fey, E.G.2    Penman, S.3    Lian, J.B.4    Stein, J.L.5    Stein, G.S.6
  • 8
    • 0028252684 scopus 로고
    • Fibroblast growth factors and their receptors: An information network controlling tissue growth, morphogenesis and repair
    • Fernig, D.G., and J.T. Gallagher. 1994. Fibroblast growth factors and their receptors: an information network controlling tissue growth, morphogenesis and repair. Prog. Growth Factor Res. 5:353-377.
    • (1994) Prog. Growth Factor Res. , vol.5 , pp. 353-377
    • Fernig, D.G.1    Gallagher, J.T.2
  • 9
    • 0022521416 scopus 로고
    • The nonchromatin substructures of the nucleus: The ribonucleoprotein (RNP)-containing and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy
    • Fey, E.G., G. Krochmalnic, and S. Penman. 1986. The nonchromatin substructures of the nucleus: The ribonucleoprotein (RNP)-containing and RNP-depleted matrices analyzed by sequential fractionation and resinless section electron microscopy. J. Cell Biol. 102:1654-1665.
    • (1986) J. Cell Biol. , vol.102 , pp. 1654-1665
    • Fey, E.G.1    Krochmalnic, G.2    Penman, S.3
  • 10
    • 0023704381 scopus 로고
    • Nuclear matrix proteins reflect cell type of origin in cultured human cells
    • Fey, E.G., and S. Penman. 1988. Nuclear matrix proteins reflect cell type of origin in cultured human cells. Proc. Natl. Acad. Sci. USA. 85:121-125.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 121-125
    • Fey, E.G.1    Penman, S.2
  • 11
    • 0025788685 scopus 로고
    • Multiple surface forms of bFGF: Differential nuclear and cell surface localization
    • Florkiewicz, R.Z., A. Baird, and A.M. Gonzalez. 1991. Multiple surface forms of bFGF: Differential nuclear and cell surface localization. Growth Factors. 4:265-275.
    • (1991) Growth Factors , vol.4 , pp. 265-275
    • Florkiewicz, R.Z.1    Baird, A.2    Gonzalez, A.M.3
  • 12
    • 0023877257 scopus 로고
    • Internalization and degradation of heparin binding growth factor-I by endothelial cells
    • Friesel, R., and T. Maciag. 1988. Internalization and degradation of heparin binding growth factor-I by endothelial cells. Biochem. Biophys. Res. Commun. 151:957-964.
    • (1988) Biochem. Biophys. Res. Commun. , vol.151 , pp. 957-964
    • Friesel, R.1    Maciag, T.2
  • 13
    • 0027050480 scopus 로고
    • Complexity of FGF receptors: Genetic basis for structural diversity and functional specificity
    • Givol, D., and A. Yayon. 1992. Complexity of FGF receptors: genetic basis for structural diversity and functional specificity. FASEB (Fed. Am. Soc. Exp. Biol.) J. 6:3362-3369.
    • (1992) FASEB (Fed. Am. Soc. Exp. Biol.) J. , vol.6 , pp. 3362-3369
    • Givol, D.1    Yayon, A.2
  • 14
    • 0028956761 scopus 로고
    • High affinity immunoreactive FGF receptors in the extracellular matrix of vascular endothelial cells - Implications for the modulation of FGF-2
    • Hanneken, A., P.A. Maher, and A. Baird. 1995. High affinity immunoreactive FGF receptors in the extracellular matrix of vascular endothelial cells - implications for the modulation of FGF-2. J Cell Biol. 128:1221-1228.
    • (1995) J. Cell Biol. , vol.128 , pp. 1221-1228
    • Hanneken, A.1    Maher, P.A.2    Baird, A.3
  • 15
    • 0028107667 scopus 로고
    • Epidermal growth factor induced tyrosine phosphorylation of nuclear proteins associated with translocation of epidermal growth factor receptors into the nucleus
    • Holt, S.J., P. Alexander, C.B. Inman, and D.E. Davies. 1994. Epidermal growth factor induced tyrosine phosphorylation of nuclear proteins associated with translocation of epidermal growth factor receptors into the nucleus. Biochem. Pharmacol. 47:117-126.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 117-126
    • Holt, S.J.1    Alexander, P.2    Inman, C.B.3    Davies, D.E.4
  • 16
    • 0028055258 scopus 로고
    • Internalization of polypeptide growth factor receptors and the regulation of transcription
    • Hopkins, C.R. 1994. Internalization of polypeptide growth factor receptors and the regulation of transcription. Biochem. Pharmacol. 47:151-154.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 151-154
    • Hopkins, C.R.1
  • 17
    • 0022396827 scopus 로고
    • Identification of surface proteins on bovine leukocytes by a biotin-avidin protein blotting technique
    • Hurley, W.L., E. Finkelstein, and B.D. Holst. 1985. Identification of surface proteins on bovine leukocytes by a biotin-avidin protein blotting technique. J. Immunol. Methods. 85:195-202.
    • (1985) J. Immunol. Methods , vol.85 , pp. 195-202
    • Hurley, W.L.1    Finkelstein, E.2    Holst, B.D.3
  • 18
    • 0025342559 scopus 로고
    • Nucleocytoplasmic transport is enhanced concomitant with nuclear accumulation of epidermal growth factor (EGF) binding activity in both 3T3-1 and EGF receptor reconstituted NR-6 fibroblasts
    • Jiang, L.-W., and M. Schindler. 1990. Nucleocytoplasmic transport is enhanced concomitant with nuclear accumulation of epidermal growth factor (EGF) binding activity in both 3T3-1 and EGF receptor reconstituted NR-6 fibroblasts. J. Cell Biol. 110:559-568.
    • (1990) J. Cell Biol. , vol.110 , pp. 559-568
    • Jiang, L.-W.1    Schindler, M.2
  • 19
    • 0027344852 scopus 로고
    • Structural and functional diversity in the FGF receptor multigene family
    • Johnson, D.E., and L.T. Williams. 1993. Structural and functional diversity in the FGF receptor multigene family. Adv. Cancer Res. 60:1-41.
    • (1993) Adv. Cancer Res. , vol.60 , pp. 1-41
    • Johnson, D.E.1    Williams, L.T.2
  • 20
    • 0029559922 scopus 로고
    • Fibroblast growth factor receptors (FGFRs) localize in different cellular compartments
    • Johnston, C.L., H.C. Cox, J.J. Gomm, and R.C. Coombes. 1995. Fibroblast growth factor receptors (FGFRs) localize in different cellular compartments. J. Biol. Chem. 270:30643-30650.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30643-30650
    • Johnston, C.L.1    Cox, H.C.2    Gomm, J.J.3    Coombes, R.C.4
  • 21
    • 0025995222 scopus 로고
    • Molecular cloning of a human basic fibroblast growth factor receptor cDNA and expression of a biologically active extracellular domain in a baculovirus system
    • Kiefer, M.C., A. Baird, T. Nguyen, C. George-Nascimento, O.B. Mason, L.J. Boley, P. Valenzuela, and P.J. Barr. 1991. Molecular cloning of a human basic fibroblast growth factor receptor cDNA and expression of a biologically active extracellular domain in a baculovirus system. Growth Factors. 5:115-127.
    • (1991) Growth Factors , vol.5 , pp. 115-127
    • Kiefer, M.C.1    Baird, A.2    Nguyen, T.3    George-Nascimento, C.4    Mason, O.B.5    Boley, L.J.6    Valenzuela, P.7    Barr, P.J.8
  • 22
    • 0028143506 scopus 로고
    • Nuclear translocation and anchorage of the growth hormone receptor
    • Lobie, P.E., T.J.J. Wood, C.M. Chen, M.J. Waters, and G. Norsted. 1994. Nuclear translocation and anchorage of the growth hormone receptor. J. Biol. Chem. 269:31735-31746.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31735-31746
    • Lobie, P.E.1    Wood, T.J.J.2    Chen, C.M.3    Waters, M.J.4    Norsted, G.5
  • 23
    • 0025967465 scopus 로고
    • Tissue-dependent regulation of protein tyrosine kinase activity during embryonic development
    • Maher, P.A. 1991. Tissue-dependent regulation of protein tyrosine kinase activity during embryonic development. J. Cell Biol. 112:955-963.
    • (1991) J. Cell Biol. , vol.112 , pp. 955-963
    • Maher, P.A.1
  • 24
    • 0027418242 scopus 로고
    • Inhibition of the tyrosine kinase activity of the fibroblast growth factor receptor by the methyltransferase inhibitor 5′-methylthioadenosine
    • Maher, P.A. 1993. Inhibition of the tyrosine kinase activity of the fibroblast growth factor receptor by the methyltransferase inhibitor 5′-methylthioadenosine. J. Biol. Chem. 268:4244-4249.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4244-4249
    • Maher, P.A.1
  • 26
    • 0024154153 scopus 로고
    • Internalization and limited processing of basic fibroblast growth factor on chinese hamster lung fibroblasts
    • Moenner, M., L. Gannoun-Zaki, J. Badet, and D. Barritault. 1989. Internalization and limited processing of basic fibroblast growth factor on chinese hamster lung fibroblasts. Growth Factors. 1:115-123.
    • (1989) Growth Factors , vol.1 , pp. 115-123
    • Moenner, M.1    Gannoun-Zaki, L.2    Badet, J.3    Barritault, D.4
  • 28
    • 0023707212 scopus 로고
    • Comparative studies of the tyrosine phosphorylation of proteins in Swiss 3T3 fibroblasts stimulated by a variety of mitogenic agents
    • Pasquale, E.B., P.A. Maher, and S.J. Singer. 1988. Comparative studies of the tyrosine phosphorylation of proteins in Swiss 3T3 fibroblasts stimulated by a variety of mitogenic agents. J. Cell. Physiol. 137:146-156.
    • (1988) J. Cell. Physiol. , vol.137 , pp. 146-156
    • Pasquale, E.B.1    Maher, P.A.2    Singer, S.J.3
  • 29
  • 31
    • 0026213963 scopus 로고
    • Basic fibroblast growth factor requires a long-lasting activation of protein kinase C to induce cell proliferation in transformed fetal aortic endothelial cells
    • Presta, M., L. Tiberio, M. Rusnati, P. Dell'Era, and G. Ragnotti. 1991. Basic fibroblast growth factor requires a long-lasting activation of protein kinase C to induce cell proliferation in transformed fetal aortic endothelial cells. Cell Reg. 2:719-726.
    • (1991) Cell Reg. , vol.2 , pp. 719-726
    • Presta, M.1    Tiberio, L.2    Rusnati, M.3    Dell'Era, P.4    Ragnotti, G.5
  • 32
    • 0028081352 scopus 로고
    • Intact and functional fibroblast growth factor (FGF) receptor-1 trafficks near the nucleus in response to FGF-1
    • Prudovsky, I., N. Savion, X. Zhan, R. Friesel, J. Xu, J. Hou, W.L. McKeehan, and T. Maciag. 1994. Intact and functional fibroblast growth factor (FGF) receptor-1 trafficks near the nucleus in response to FGF-1. J. Biol. Chem. 269:31720-31724.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31720-31724
    • Prudovsky, I.1    Savion, N.2    Zhan, X.3    Friesel, R.4    Xu, J.5    Hou, J.6    McKeehan, W.L.7    Maciag, T.8
  • 33
    • 0024591960 scopus 로고
    • Epidermal growth factor (EGF) and monoclonal antibody to cell surface EGF receptor bind to the same chromatin receptor
    • Rakowicz-Szulczynska, E.M., D. Otwiaska, U. Rodeck, and H. Koprowski. 1989. Epidermal growth factor (EGF) and monoclonal antibody to cell surface EGF receptor bind to the same chromatin receptor. Archiv. Biochem. Biophys. 268:456-464.
    • (1989) Archiv. Biochem. Biophys. , vol.268 , pp. 456-464
    • Rakowicz-Szulczynska, E.M.1    Otwiaska, D.2    Rodeck, U.3    Koprowski, H.4
  • 34
    • 0025331365 scopus 로고
    • Nuclear and cytoplasmic localization of different basic fibroblast growth factor species
    • Renko, M., N. Quarto, T. Morimoto, and D.B. Rifkin. 1990. Nuclear and cytoplasmic localization of different basic fibroblast growth factor species. J. Cell. Physiol. 144:108-114.
    • (1990) J. Cell. Physiol. , vol.144 , pp. 108-114
    • Renko, M.1    Quarto, N.2    Morimoto, T.3    Rifkin, D.B.4
  • 35
    • 0024380087 scopus 로고
    • Rapid detection of octamer binding proteins with 'mini-extracts' prepared from a small number of cells
    • Schreiber, E., P. Matthias, M.M. Muller, and W. Schaffner. 1989. Rapid detection of octamer binding proteins with 'mini-extracts' prepared from a small number of cells. Nucleic. Acids Res. 17:6419.
    • (1989) Nucleic. Acids Res. , vol.17 , pp. 6419
    • Schreiber, E.1    Matthias, P.2    Muller, M.M.3    Schaffner, W.4
  • 36
    • 0026022910 scopus 로고
    • How proteins enter the nucleus
    • Silver, P.A. 1991. How proteins enter the nucleus. Cell. 64:489-497.
    • (1991) Cell , vol.64 , pp. 489-497
    • Silver, P.A.1
  • 38
    • 0025202476 scopus 로고
    • Basic fibroblast growth factor accumulates in the nuclei of various bFGF-producing cell types
    • Tessler, S., and G. Neufeld. 1990. Basic fibroblast growth factor accumulates in the nuclei of various bFGF-producing cell types. J. Cell. Physiol. 145:310-317.
    • (1990) J. Cell. Physiol. , vol.145 , pp. 310-317
    • Tessler, S.1    Neufeld, G.2
  • 39
    • 0026061098 scopus 로고
    • The fibroblast growth factors: An emerging family of neural growth factors
    • Wagner, J.A. 1991. The fibroblast growth factors: an emerging family of neural growth factors. Curr. Top. Microbiol. Immunol. 165:95-118.
    • (1991) Curr. Top. Microbiol. Immunol. , vol.165 , pp. 95-118
    • Wagner, J.A.1
  • 40
    • 0026055903 scopus 로고
    • Internalization and processing of basic fibroblast growth factor by neurons and astrocytes
    • Walicke, P.A., and A. Baird. 1991. Internalization and processing of basic fibroblast growth factor by neurons and astrocytes. J. Neurosci. 11:2249-2258.
    • (1991) J. Neurosci. , vol.11 , pp. 2249-2258
    • Walicke, P.A.1    Baird, A.2
  • 41
    • 0028328846 scopus 로고
    • Dual mode of signal transduction by externally added acidic fibroblast growth factor
    • Wiedlocha, A., P.O. Falnes, I.H. Madshus, K. Sandvig, and S. Olsnes. 1994. Dual mode of signal transduction by externally added acidic fibroblast growth factor. Cell. 76:1039-1051.
    • (1994) Cell , vol.76 , pp. 1039-1051
    • Wiedlocha, A.1    Falnes, P.O.2    Madshus, I.H.3    Sandvig, K.4    Olsnes, S.5
  • 42
    • 0028170686 scopus 로고
    • neu tyrosine kinase and its association with transcriptional transactivation
    • neu tyrosine kinase and its association with transcriptional transactivation. Biochem. Biophys. Res. Commun. 203:1589-1598.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1589-1598
    • Xie, Y.1    Hung, M.-C.2
  • 43
    • 0026469173 scopus 로고
    • Analysis of endogenous and exogenous nuclear translocation of fibroblast growth factor-1 in NIH 3T3 cells
    • Zhan, X., X. Hu, S. Friedman, and T. Maciag. 1992. Analysis of endogenous and exogenous nuclear translocation of fibroblast growth factor-1 in NIH 3T3 cells. Biochem. Biophys. Res. Commun. 188:982-991.
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 982-991
    • Zhan, X.1    Hu, X.2    Friedman, S.3    Maciag, T.4
  • 44
    • 0027286319 scopus 로고
    • Long term growth factor exposure and differential tyrosine phosphorylation are required for DNA synthesis in Balb/C 3T3 cells
    • Zhan, X., X. Hu, R. Friesel, and T. Maciag. 1993. Long term growth factor exposure and differential tyrosine phosphorylation are required for DNA synthesis in Balb/C 3T3 cells. J. Biol. Chem. 268:9611-9620.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9611-9620
    • Zhan, X.1    Hu, X.2    Friesel, R.3    Maciag, T.4


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