메뉴 건너뛰기




Volumn 50, Issue 40, 2011, Pages 8576-8582

The physical basis of FGFR3 response to fgf1 and fgf2

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION LOOPS; ALTERNATIVE SPLICING; BIOLOGICAL RESPONSE; BONE DEVELOPMENT; EMBRYONIC DEVELOPMENT; FIBROBLAST GROWTH FACTOR; FIBROBLAST GROWTH FACTOR RECEPTORS; GAIN INSIGHT; ISOFORMS; MEMBRANE RECEPTORS;

EID: 80053578487     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200986f     Document Type: Article
Times cited : (23)

References (46)
  • 1
    • 18144383021 scopus 로고    scopus 로고
    • Cellular signaling by fibroblast growth factor receptors
    • DOI 10.1016/j.cytogfr.2005.01.001
    • Eswarakumar, V. P., Lax, I., and Schlessinger, J. (2005) Cellular signaling by fibroblast growth factor receptors Cytokine Growth Factor Rev. 16, 139-149 (Pubitemid 40616112)
    • (2005) Cytokine and Growth Factor Reviews , vol.16 , Issue.2 SPEC. ISS. , pp. 139-149
    • Eswarakumar, V.P.1    Lax, I.2    Schlessinger, J.3
  • 2
    • 0029294653 scopus 로고
    • Functions of fibroblast growth factors and their receptors
    • Wilkie, A. O. M., Morriss-Kay, G. M., Jones, E. Y., and Heath, J. K. (1995) Functions of fibroblast growth factors and their receptors Curr. Biol. 5, 500-507
    • (1995) Curr. Biol. , vol.5 , pp. 500-507
    • Wilkie, A.O.M.1    Morriss-Kay, G.M.2    Jones, E.Y.3    Heath, J.K.4
  • 4
    • 0016318749 scopus 로고
    • Localization of A Fibroblast Growth-Factor and Its Effect Alone and with Hydrocortisone on 3T3 Cell-Growth
    • GOSPODAR, D. (1974) Localization of A Fibroblast Growth-Factor and Its Effect Alone and with Hydrocortisone on 3T3 Cell-Growth Nature 249, 123-127
    • (1974) Nature , vol.249 , pp. 123-127
    • Gospodar, D.1
  • 5
    • 0016704918 scopus 로고
    • Purification of A Fibroblast Growth-Factor from Bovine Pituitary
    • Gospodarowicz, D. (1975) Purification of A Fibroblast Growth-Factor from Bovine Pituitary J. Biol. Chem. 250, 2515-2520
    • (1975) J. Biol. Chem. , vol.250 , pp. 2515-2520
    • Gospodarowicz, D.1
  • 6
    • 0017822597 scopus 로고
    • Purification of the fibroblast growth factor activity from bovine brain
    • Gospodarowicz, D., Bialecki, H., and Greenburg, G. (1978) Purification of Fibroblast Growth-Factor Activity from Bovine Brain J. Biol. Chem. 253, 3736-3743 (Pubitemid 8346572)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.10 , pp. 3736-3743
    • Gospodarowicz, D.1    Bialecki, H.2    Greenburg, G.3
  • 8
    • 0026548976 scopus 로고
    • Basic Fibroblast Growth-Factor, A Protein Devoid of Secretory Signal Sequence, Is Released by Cells Via A Pathway Independent of the Endoplasmic-Reticulum Golgi-Complex
    • Mignatti, P., Morimoto, T., and Rifkin, D. B. (1992) Basic Fibroblast Growth-Factor, A Protein Devoid of Secretory Signal Sequence, Is Released by Cells Via A Pathway Independent of the Endoplasmic-Reticulum Golgi-Complex J. Cell. Physiol. 151, 81-93
    • (1992) J. Cell. Physiol. , vol.151 , pp. 81-93
    • Mignatti, P.1    Morimoto, T.2    Rifkin, D.B.3
  • 10
    • 0023269163 scopus 로고
    • High and low affinity binding sites for basic fibroblast growth factor on cultured cells: Absence of a role for low affinity binding in the stimulation of plasminogen activator production by bovine capillary endothelial cells
    • DOI 10.1002/jcp.1041310118
    • Moscatelli, D. (1987) High and Low Affinity Binding-Sites for Basic Fibroblast Growth-Factor on Cultured-Cells-Absence of A Role for Low Affinity Binding in the Stimulation of Plasminogen-Activator Production by Bovine Capillary Endothelial-Cells J. Cell. Physiol. 131, 123-130 (Pubitemid 17067272)
    • (1987) Journal of Cellular Physiology , vol.131 , Issue.1 , pp. 123-130
    • Moscatelli, D.1
  • 11
    • 0026502460 scopus 로고
    • Heparin Is Required for Cell-Free Binding of Basic Fibroblast Growth-Factor to A Soluble Receptor and for Mitogenesis in Whole Cells
    • Ornitz, D. M., Yayon, A., Flanagan, J. G., Svahn, C. M., Levi, E., and Leder, P. (1992) Heparin Is Required for Cell-Free Binding of Basic Fibroblast Growth-Factor to A Soluble Receptor and for Mitogenesis in Whole Cells Mol. Cell. Biol. 12, 240-247
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 240-247
    • Ornitz, D.M.1    Yayon, A.2    Flanagan, J.G.3    Svahn, C.M.4    Levi, E.5    Leder, P.6
  • 12
    • 0025976838 scopus 로고
    • Cell surface, heparin-like molecules are required for binding of basic fibroblast growth factor to its high affinity receptor
    • Yayon, A., Klagsbrun, M., Esko, J. D., Leder, P., and Ornitz, D. M. (1991) Cell-Surface, Heparin-Like Molecules Are Required for Binding of Basic Fibroblast Growth-Factor to Its High-Affinity Receptor Cell 64, 841-848 (Pubitemid 121001170)
    • (1991) Cell , vol.64 , Issue.4 , pp. 841-848
    • Yayon, A.1    Klagsbrun, M.2    Esko, J.D.3    Leder, P.4    Ornitz, D.M.5
  • 13
    • 0032841757 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development
    • Lin, X. H., Buff, E. M., Perrimon, N., and Michelson, A. M. (1999) Heparan sulfate proteoglycans are essential for FGF receptor signaling during Drosophila embryonic development Development 126, 3715-3723 (Pubitemid 29440471)
    • (1999) Development , vol.126 , Issue.17 , pp. 3715-3723
    • Lin, X.1    Buff, E.M.2    Perrimon, N.3    Michelson, A.M.4
  • 14
    • 0033520472 scopus 로고    scopus 로고
    • Structural basis for FGF receptor dimerization and activation
    • DOI 10.1016/S0092-8674(00)80051-3
    • Plotnikov, A. N., Schlessinger, J., Hubbard, S. R., and Mohammadi, M. (1999) Structural basis for FGF receptor dimerization and activation Cell 98, 641-650 (Pubitemid 29418955)
    • (1999) Cell , vol.98 , Issue.5 , pp. 641-650
    • Plotnikov, A.N.1    Schlessinger, J.2    Hubbard, S.R.3    Mohammadi, M.4
  • 15
    • 0034640103 scopus 로고    scopus 로고
    • Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity
    • Plotnikov, A. N., Hubbard, S. R., Schlessinger, J., and Mohammadi, M. (2000) Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity Cell 101, 413-424
    • (2000) Cell , vol.101 , pp. 413-424
    • Plotnikov, A.N.1    Hubbard, S.R.2    Schlessinger, J.3    Mohammadi, M.4
  • 16
    • 18144423534 scopus 로고    scopus 로고
    • Structural basis for fibroblast growth factor receptor activation
    • DOI 10.1016/j.cytogfr.2005.01.008
    • Mohammadi, M., Olsen, S. K., and Ibrahimi, O. A. (2005) Structural basis for fibroblast growth factor receptor activation Cytokine Growth Factor Rev. 16, 107-137 (Pubitemid 40616111)
    • (2005) Cytokine and Growth Factor Reviews , vol.16 , Issue.2 SPEC. ISS. , pp. 107-137
    • Mohammadi, M.1    Olsen, S.K.2    Ibrahimi, O.A.3
  • 17
    • 0033951768 scopus 로고    scopus 로고
    • FGFs, heparan sulfate and FGFRs: Complex interactions essential for development
    • DOI 10.1002/(SICI)1521-1878(200002)22: 2<108::AID-BIES2>3.0.CO;2-M
    • Ornitz, D. M. (2000) FGFs, heparan sulfate and FGFRs: complex interactions essential for development BioEssays 22, 108-112 (Pubitemid 30092077)
    • (2000) BioEssays , vol.22 , Issue.2 , pp. 108-112
    • Ornitz, D.M.1
  • 18
    • 14644394929 scopus 로고    scopus 로고
    • Cell responses to FGFR3 signalling: Growth, differentiation and apoptosis
    • DOI 10.1016/j.yexcr.2004.11.012
    • L'Horte, C. G. M. and Knowles, M. A. (2005) Cell responses to FGFR3 signaling: growth, differentiation and apoptosis. Experim Cell Res. 304, 417-431 (Pubitemid 40321120)
    • (2005) Experimental Cell Research , vol.304 , Issue.2 , pp. 417-431
    • L'Hote, C.G.M.1    Knowles, M.A.2
  • 19
    • 5444250989 scopus 로고    scopus 로고
    • Biochemical analysis of pathogenic ligand-dependent FGFR2 mutations suggests distinct pathophysiological mechanisms for craniofacial and limb abnormalities
    • DOI 10.1093/hmg/ddh235
    • Ibrahimi, O. A., Zhang, F. M., Eliseenkova, A. V., Itoh, N., Linhardt, R. J., and Mohammadi, M. (2004) Biochemical analysis of pathogenic ligand-dependent FGFR2 mutations suggests distinct pathophysiological mechanisms for craniofacial and limb abnormalities Hum. Mol. Genet. 13, 2313-2324 (Pubitemid 39359928)
    • (2004) Human Molecular Genetics , vol.13 , Issue.19 , pp. 2313-2324
    • Ibrahimi, O.A.1    Zhang, F.2    Eliseenkova, A.V.3    Itoh, N.4    Linhardt, R.J.5    Mohammadi, M.6
  • 20
    • 0347287038 scopus 로고    scopus 로고
    • Proline to arginine mutations in FGF receptors 1 and 3 result in Pfeiffer and Muenke craniosynostosis syndromes through enhancement of FGF binding affinity
    • DOI 10.1093/hmg/ddh011
    • Ibrahimi, O. A., Zhang, F. M., Eliseenkova, A. V., Linhardt, R. J., and Mohammadi, M. (2004) Proline to arginine mutations in FGF receptors 1 and 3 result in Pfeiffer and Muenke craniosynostosis syndromes through enhancement of FGF binding affinity Hum. Mol. Genet. 13, 69-78 (Pubitemid 38072136)
    • (2004) Human Molecular Genetics , vol.13 , Issue.1 , pp. 69-78
    • Ibrahimi, O.A.1    Zhang, F.2    Eliseenkova, A.V.3    Linhardt, R.J.4    Mohammadi, M.5
  • 22
    • 33744937606 scopus 로고    scopus 로고
    • Receptor specificity of the fibroblast growth factor family: The complete mammalian FGF family
    • DOI 10.1074/jbc.M601252200
    • Zhang, X. Q., Ibrahimi, O. A., Olsen, S. K., Umemori, H., Mohammadi, M., and Ornitz, D. M. (2006) Receptor specificity of the fibroblast growth factor family-The complete mammalian FGF family J. Biol. Chem. 281, 15694-15700 (Pubitemid 43848456)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.23 , pp. 15694-15700
    • Zhang, X.1    Ibrahimi, O.A.2    Olsen, S.K.3    Umemori, H.4    Mohammadi, M.5    Ornitz, D.M.6
  • 25
    • 0034464005 scopus 로고    scopus 로고
    • The molecular and genetic basis of fibroblast growth factor receptor 3 disorders: The achondroplasia family of skeletal dysplasias, Muenke craniosynostosis, and Crouzon syndrome with acanthosis nigricans
    • DOI 10.1210/er.21.1.23
    • Vajo, Z., Francomano, C. A., and Wilkin, D. J. (2000) The molecular and genetic basis of fibroblast growth factor receptor 3 disorders: The achondroplasia family of skeletal dysplasias, Muenke craniosynostosis, and Crouzon syndrome with acanthosis nigricans Endocrine Rev. 21, 23-39 (Pubitemid 32260394)
    • (2000) Endocrine Reviews , vol.21 , Issue.1 , pp. 23-39
    • Vajo, Z.1    Francomano, C.A.2    Wilkin, D.J.3
  • 26
    • 0027964261 scopus 로고
    • Mutations in the transmembrane domain of FGFR3 cause the most common genetic form of dwarfism, achondroplasia
    • DOI 10.1016/0092-8674(94)90302-6
    • Shiang, R., Thompson, L. M., Zhu, Y.-Z., Church, D. M., Fielder, T. J., Bocian, M., Winokur, S. T., and Wasmuth, J. J. (1994) Mutations in the transmembrane domain of FGFR3 cause the most common genetic form of dwarfism, achondroplasia Cell 78, 335-342 (Pubitemid 24241100)
    • (1994) Cell , vol.78 , Issue.2 , pp. 335-342
    • Shiang, R.1    Thompson, L.M.2    Zhu, Y.-Z.3    Church, D.M.4    Fielder, T.J.5    Bocian, M.6    Winokur, S.T.7    Wasmuth, J.J.8
  • 28
    • 0029935895 scopus 로고    scopus 로고
    • Graded activation of fibroblast growth factor receptor 3 by mutations causing achondroplasia and thanatophoric dysplasia
    • DOI 10.1038/ng0696-233
    • Naski, M. C., Wang, Q., Xu, J. S., and Ornitz, D. M. (1996) Graded activation of fibroblast growth factor receptor 3 by mutations causing achondroplasia and thanatophoric dysplasia Nature Genet. 13, 233-237 (Pubitemid 26166160)
    • (1996) Nature Genetics , vol.13 , Issue.2 , pp. 233-237
    • Naski, M.C.1    Wang, Q.2    Xu, J.3    Ornitz, D.M.4
  • 31
    • 77956907848 scopus 로고    scopus 로고
    • The physical basis behind achondroplasia, the most common form of human dwarfism
    • He, L., Horton, W. A., and Hristova, K. (2010) The physical basis behind achondroplasia, the most common form of human dwarfism J. Biol. Chem. 285, 30103-30114
    • (2010) J. Biol. Chem. , vol.285 , pp. 30103-30114
    • He, L.1    Horton, W.A.2    Hristova, K.3
  • 32
    • 31344468061 scopus 로고    scopus 로고
    • FGFR3 dimer stabilization due to a single amino acid pathogenic mutation
    • DOI 10.1016/j.jmb.2005.11.077, PII S0022283605015135
    • Li, E., You, M., and Hristova, K. (2006) FGFR3 dimer stabilization due to a single amino acid pathogenic mutation J. Mol. Biol. 356, 600-612 (Pubitemid 43139323)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.3 , pp. 600-612
    • Li, E.1    You, M.2    Hristova, K.3
  • 33
    • 34848865082 scopus 로고    scopus 로고
    • Effect of pathogenic cysteine mutations on FGFR3 transmembrane domain dimerization in detergents and lipid bilayers
    • DOI 10.1021/bi700986n
    • You, M., Spangler, J., Li, E., Han, X., Ghosh, P., and Hristova, K. (2007) Effect of pathogenic cysteine mutations on FGFR3 transmembrane domain dimerization in detergents and lipid bilayers Biochemistry 46, 11039-11046 (Pubitemid 47502770)
    • (2007) Biochemistry , vol.46 , Issue.39 , pp. 11039-11046
    • You, M.1    Spangler, J.2    Li, E.3    Han, X.4    Ghosh, P.5    Hristova, K.6
  • 34
    • 33646347414 scopus 로고    scopus 로고
    • The achondroplasia mutation does not alter the dimerization energetics of the fibroblast growth factor receptor 3 transmembrane domain
    • DOI 10.1021/bi060113g
    • You, M., Li, E., and Hristova, K. (2006) The achondroplasia mutation does not alter the dimerization energetics of FGFR3 transmembrane domain Biochemistry 45, 5551-5556 (Pubitemid 43673185)
    • (2006) Biochemistry , vol.45 , Issue.17 , pp. 5551-5556
    • You, M.1    Li, E.2    Hristova, K.3
  • 35
    • 0033981302 scopus 로고    scopus 로고
    • The transmembrane mutation G380R in fibroblast growth factor receptor 3 uncouples ligand-mediated receptor activation from down-regulation
    • DOI 10.1128/MCB.20.2.516-522.2000
    • Monsonego-Ornan, E., Adar, R., Feferman, T., Segev, O., and Yayon, A. (2000) The transmembrane mutation G380R in fibroblast growth factor receptor 3 uncouples ligand-mediated receptor activation from down-regulation Mol. Cell. Biol. 20, 516-522 (Pubitemid 30023093)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.2 , pp. 516-522
    • Monsonego-Ornan, E.1    Adar, R.2    Feferman, T.3    Segev, O.4    Yayon, A.5
  • 36
    • 0037174151 scopus 로고    scopus 로고
    • FGF receptors ubiquitylation: Dependence on tyrosine kinase activity and role in downregulation
    • DOI 10.1016/S0014-5793(02)03255-6, PII S0014579302032556
    • Monsonego-Ornan, E., Adar, R., Rom, E., and Yayon, A. (2002) FGF receptors ubiquitylation: dependence on tyrosine kinase activity and role in downregulation FEBS Lett. 528, 83-89 (Pubitemid 35258004)
    • (2002) FEBS Letters , vol.528 , Issue.1-3 , pp. 83-89
    • Monsonego-Ornan, E.1    Adar, R.2    Rom, E.3    Yayon, A.4
  • 37
    • 0036239904 scopus 로고    scopus 로고
    • Differential activation of cysteine-substitution mutants of fibroblast growth factor receptor 3 is determined by cysteine localization
    • Adar, R., Monsonego-Ornan, E., David, P., and Yayon, A. (2002) Differential activation of cysteine-substitution mutants of fibroblast growth factor receptor 3 is determined by cysteine localization J. Bone Miner. Res. 17, 860-868 (Pubitemid 34441903)
    • (2002) Journal of Bone and Mineral Research , vol.17 , Issue.5 , pp. 860-868
    • Adar, R.1    Monsonego-Ornan, E.2    David, P.3    Yayon, A.4
  • 38
    • 79953856862 scopus 로고    scopus 로고
    • FGFR3 heterodimerization in achondroplasia, the most common form of human dwarfism
    • He, L., Wimley, W. C., and Hristova, K. (2011) FGFR3 heterodimerization in achondroplasia, the most common form of human dwarfism J. Biol. Chem. 286, 13272-13281
    • (2011) J. Biol. Chem. , vol.286 , pp. 13272-13281
    • He, L.1    Wimley, W.C.2    Hristova, K.3
  • 39
    • 0033520935 scopus 로고    scopus 로고
    • Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules: Multiple regions determine ligand binding specificity
    • Chellaiah, A., Yuan, W. L., Chellaiah, M., and Ornitz, D. M. (1999) Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules-Multiple regions determine ligand binding specificity J. Biol. Chem. 274, 34785-34794 (Pubitemid 129509522)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.49 , pp. 34785-34794
    • Chellaiah, A.1    Yuan, W.2    Chellaiah, M.3    Ornitz, D.M.4
  • 40
    • 56949102246 scopus 로고    scopus 로고
    • Pathogenic activation of receptor tyrosine kinases in mammalian membranes
    • He, L. and Hristova, K. (2008) Pathogenic activation of receptor tyrosine kinases in mammalian membranes J. Mol. Biol. 384, 1130-1142
    • (2008) J. Mol. Biol. , vol.384 , pp. 1130-1142
    • He, L.1    Hristova, K.2
  • 41
    • 33745474608 scopus 로고    scopus 로고
    • Insights into the role of heparan sulphate in fibroblast growth factor signalling
    • DOI 10.1042/BST0340442
    • Harmer, N. J. (2006) Insights into the role of heparan sulphate in fibroblast growth factor signalling Biochem. Soc. Trans. 34, 442-445 (Pubitemid 43954007)
    • (2006) Biochemical Society Transactions , vol.34 , Issue.3 , pp. 442-445
    • Harmer, N.J.1
  • 43
    • 0030027488 scopus 로고    scopus 로고
    • Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction
    • Mohammadi, M., Dikic, I., Sorokin, A., Burgess, W. H., Jaye, M., and Schlessinger, J. (1996) Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction Mol. Cell. Biol. 16, 977-989 (Pubitemid 26061669)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.3 , pp. 977-989
    • Mohammadi, M.1    Dikic, I.2    Sorokin, A.3    Burgess, W.H.4    Jaye, M.5    Schlessinger, J.6
  • 44
    • 0032567346 scopus 로고    scopus 로고
    • Effect of transmembrane and kinase domain mutations on fibroblast growth factor receptor 3 chimera signaling in PC12 cells. A model for the control of receptor tyrosine kinase activation
    • DOI 10.1074/jbc.273.52.35250
    • Raffioni, S., Zhu, Y. Z., Bradshaw, R. A., and Thompson, L. M. (1998) Effect of transmembrane and kinase domain mutations on fibroblast growth factor receptor 3 chimera signaling in PC12 cells. A model for the control of receptor tyrosine kinase activation J. Biol. Chem. 273, 35250-35259 (Pubitemid 29028232)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.52 , pp. 35250-35259
    • Raffioni, S.1    Zhu, Y.-Z.2    Bradshaw, R.A.3    Thompson, L.M.4
  • 45
    • 33745002702 scopus 로고    scopus 로고
    • An Allosteric Mechanism for Activation of the Kinase Domain of Epidermal Growth Factor Receptor
    • DOI 10.1016/j.cell.2006.05.013, PII S0092867406005848
    • Zhang, X. W., Gureasko, J., Shen, K., Cole, P. A., and Kuriyan, J. (2006) An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor Cell 125, 1137-1149 (Pubitemid 43866200)
    • (2006) Cell , vol.125 , Issue.6 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 46
    • 77649251478 scopus 로고    scopus 로고
    • Asymmetric receptor contact is required for tyrosine autophosphorylation of fibroblast growth factor receptor in living cells
    • Bae, J. H., Boggon, T. J., Tome, F., Mandiyan, V., Lax, I., and Schlessinger, J. (2010) Asymmetric receptor contact is required for tyrosine autophosphorylation of fibroblast growth factor receptor in living cells Proc. Natl. Acad. Sci. U. S. A. 107, 2866-2871
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 2866-2871
    • Bae, J.H.1    Boggon, T.J.2    Tome, F.3    Mandiyan, V.4    Lax, I.5    Schlessinger, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.