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Volumn 10, Issue 5, 2015, Pages 1319-1329

Illuminating the molecular ,mechanisms of tyrosine kinase inhibitor resistance for the FGFR1 gatekeeper mutation: The Achilles' heel of targeted therapy

Author keywords

[No Author keywords available]

Indexed keywords

AZD 4547; FIBROBLAST GROWTH FACTOR RECEPTOR 1; LUCITANIB; PROTEIN TYROSINE KINASE INHIBITOR; FGFR1 PROTEIN, HUMAN; PROTEIN KINASE INHIBITOR; PROTEIN TYROSINE KINASE;

EID: 84929577575     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.5b00014     Document Type: Article
Times cited : (63)

References (52)
  • 1
    • 75149170979 scopus 로고    scopus 로고
    • Fibroblast growth factor signalling: From development to cancer
    • Turner, N. and Grose, R. (2010) Fibroblast growth factor signalling: from development to cancer Nat. Rev. Cancer 10, 116-129
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 116-129
    • Turner, N.1    Grose, R.2
  • 2
    • 84857433085 scopus 로고    scopus 로고
    • Mechanisms of FGFR-mediated carcinogenesis
    • Ahmad, I., Iwata, T., and Leung, H. Y. (2012) Mechanisms of FGFR-mediated carcinogenesis Biochim. Biophys. Acta 1823, 850-860
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 850-860
    • Ahmad, I.1    Iwata, T.2    Leung, H.Y.3
  • 3
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon, M. A. and Schlessinger, J. (2010) Cell signaling by receptor tyrosine kinases Cell 141, 1117-1134
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 4
    • 33344455174 scopus 로고    scopus 로고
    • Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction
    • Furdui, C. M., Lew, E. D., Schlessinger, J., and Anderson, K. S. (2006) Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction Mol. Cell 21, 711-717
    • (2006) Mol. Cell , vol.21 , pp. 711-717
    • Furdui, C.M.1    Lew, E.D.2    Schlessinger, J.3    Anderson, K.S.4
  • 6
    • 84864401436 scopus 로고    scopus 로고
    • Fibroblast growth factor receptors in breast cancer: Expression, downstream effects, and possible drug targets
    • Tenhagen, M., van Diest, P. J., Ivanova, I. A., van der Wall, E., and van der Groep, P. (2012) Fibroblast growth factor receptors in breast cancer: expression, downstream effects, and possible drug targets Endocr. Relat. Cancer 19, R115-R129
    • (2012) Endocr. Relat. Cancer , vol.19 , pp. 115-R129
    • Tenhagen, M.1    Van Diest, P.J.2    Ivanova, I.A.3    Van Der Wall, E.4    Van Der Groep, P.5
  • 7
    • 77953679934 scopus 로고    scopus 로고
    • The precise sequence of FGF receptor autophosphorylation is kinetically driven and is disrupted by oncogenic mutations
    • Lew, E. D., Furdui, C. M., Anderson, K. S., and Schlessinger, J. (2009) The precise sequence of FGF receptor autophosphorylation is kinetically driven and is disrupted by oncogenic mutations Sci. Signal. 2, ra6
    • (2009) Sci. Signal. , vol.2 , pp. 6
    • Lew, E.D.1    Furdui, C.M.2    Anderson, K.S.3    Schlessinger, J.4
  • 8
    • 79955667838 scopus 로고    scopus 로고
    • Targeting mutant fibroblast growth factor receptors in cancer
    • Greulich, H. and Pollock, P. M. (2011) Targeting mutant fibroblast growth factor receptors in cancer Trends Mol. Med. 17, 283-292
    • (2011) Trends Mol. Med. , vol.17 , pp. 283-292
    • Greulich, H.1    Pollock, P.M.2
  • 12
    • 84921373464 scopus 로고    scopus 로고
    • DFG-out mode of inhibition by an irreversible type-1 inhibitor capable of overcoming gate-keeper mutations in FGF receptors
    • Huang, Z., Tan, L., Wang, H., Liu, Y., Blais, S., Deng, J., Neubert, T. A., Gray, N. S., Li, X., and Mohammadi, M. (2014) DFG-out mode of inhibition by an irreversible type-1 inhibitor capable of overcoming gate-keeper mutations in FGF receptors ACS Chem. Biol. 10, 299-309
    • (2014) ACS Chem. Biol. , vol.10 , pp. 299-309
    • Huang, Z.1    Tan, L.2    Wang, H.3    Liu, Y.4    Blais, S.5    Deng, J.6    Neubert, T.A.7    Gray, N.S.8    Li, X.9    Mohammadi, M.10
  • 14
    • 84894054642 scopus 로고    scopus 로고
    • FGFR1 kinase inhibitors: Close regioisomers adopt divergent binding modes and display distinct biophysical signatures
    • Klein, T., Tucker, J., Holdgate, G. A., Norman, R. A., and Breeze, A. L. (2014) FGFR1 kinase inhibitors: close regioisomers adopt divergent binding modes and display distinct biophysical signatures ACS Med. Chem. Lett. 5, 166-171
    • (2014) ACS Med. Chem. Lett. , vol.5 , pp. 166-171
    • Klein, T.1    Tucker, J.2    Holdgate, G.A.3    Norman, R.A.4    Breeze, A.L.5
  • 16
    • 77649196704 scopus 로고    scopus 로고
    • Discovery of novel fibroblast growth factor receptor 1 kinase inhibitors by structure-based virtual screening
    • Ravindranathan, K. P., Mandiyan, V., Ekkati, A. R., Bae, J. H., Schlessinger, J., and Jorgensen, W. L. (2010) Discovery of novel fibroblast growth factor receptor 1 kinase inhibitors by structure-based virtual screening J. Med. Chem. 53, 1662-1672
    • (2010) J. Med. Chem. , vol.53 , pp. 1662-1672
    • Ravindranathan, K.P.1    Mandiyan, V.2    Ekkati, A.R.3    Bae, J.H.4    Schlessinger, J.5    Jorgensen, W.L.6
  • 21
    • 77950573400 scopus 로고    scopus 로고
    • Through the "gatekeeper door": Exploiting the active kinase conformation
    • Zuccotto, F., Ardini, E., Casale, E., and Angiolini, M. (2010) Through the "gatekeeper door": exploiting the active kinase conformation J. Med. Chem. 53, 2681-2694
    • (2010) J. Med. Chem. , vol.53 , pp. 2681-2694
    • Zuccotto, F.1    Ardini, E.2    Casale, E.3    Angiolini, M.4
  • 23
    • 67649726156 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Contributions from structure to clinical compounds
    • Johnson, L. N. (2009) Protein kinase inhibitors: contributions from structure to clinical compounds Q. Rev. Biophys. 42, 1-40
    • (2009) Q. Rev. Biophys. , vol.42 , pp. 1-40
    • Johnson, L.N.1
  • 24
    • 68049110634 scopus 로고    scopus 로고
    • The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site
    • Bae, J. H., Lew, E. D., Yuzawa, S., Tome, F., Lax, I., and Schlessinger, J. (2009) The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site Cell 138, 514-524
    • (2009) Cell , vol.138 , pp. 514-524
    • Bae, J.H.1    Lew, E.D.2    Yuzawa, S.3    Tome, F.4    Lax, I.5    Schlessinger, J.6
  • 25
    • 84855503769 scopus 로고    scopus 로고
    • The rise and fall of gatekeeper mutations? the BCR-ABL1 T315I paradigm
    • Gibbons, D. L., Pricl, S., Kantarjian, H., Cortes, J., and Quintas-Cardama, A. (2012) The rise and fall of gatekeeper mutations? The BCR-ABL1 T315I paradigm Cancer 118, 293-299
    • (2012) Cancer , vol.118 , pp. 293-299
    • Gibbons, D.L.1    Pricl, S.2    Kantarjian, H.3    Cortes, J.4    Quintas-Cardama, A.5
  • 28
    • 84879417823 scopus 로고    scopus 로고
    • Tumour cell responses to new fibroblast growth factor receptor tyrosine kinase inhibitors and identification of a gatekeeper mutation in FGFR3 as a mechanism of acquired resistance
    • Chell, V., Balmanno, K., Little, A. S., Wilson, M., Andrews, S., Blockley, L., Hampson, M., Gavine, P. R., and Cook, S. J. (2013) Tumour cell responses to new fibroblast growth factor receptor tyrosine kinase inhibitors and identification of a gatekeeper mutation in FGFR3 as a mechanism of acquired resistance Oncogene 32, 3059-3070
    • (2013) Oncogene , vol.32 , pp. 3059-3070
    • Chell, V.1    Balmanno, K.2    Little, A.S.3    Wilson, M.4    Andrews, S.5    Blockley, L.6    Hampson, M.7    Gavine, P.R.8    Cook, S.J.9
  • 29
    • 2642558897 scopus 로고    scopus 로고
    • Characterization of a conserved structural determinant controlling protein kinase sensitivity to selective inhibitors
    • Blencke, S., Zech, B., Engkvist, O., Greff, Z., Orfi, L., Horvath, Z., Keri, G., Ullrich, A., and Daub, H. (2004) Characterization of a conserved structural determinant controlling protein kinase sensitivity to selective inhibitors Chem. Biol. 11, 691-701
    • (2004) Chem. Biol. , vol.11 , pp. 691-701
    • Blencke, S.1    Zech, B.2    Engkvist, O.3    Greff, Z.4    Orfi, L.5    Horvath, Z.6    Keri, G.7    Ullrich, A.8    Daub, H.9
  • 30
    • 80052437758 scopus 로고    scopus 로고
    • New strategies in overcoming acquired resistance to epidermal growth factor receptor tyrosine kinase inhibitors in lung cancer
    • Oxnard, G. R., Arcila, M. E., Chmielecki, J., Ladanyi, M., Miller, V. A., and Pao, W. (2011) New strategies in overcoming acquired resistance to epidermal growth factor receptor tyrosine kinase inhibitors in lung cancer Clin. Cancer Res. 17, 5530-5537
    • (2011) Clin. Cancer Res. , vol.17 , pp. 5530-5537
    • Oxnard, G.R.1    Arcila, M.E.2    Chmielecki, J.3    Ladanyi, M.4    Miller, V.A.5    Pao, W.6
  • 32
    • 84914094459 scopus 로고    scopus 로고
    • Structural insights into FGFR kinase isoform selectivity: Diverse binding modes of AZD4547 and ponatinib in complex with FGFR1 and FGFR4
    • Tucker, J. A., Klein, T., Breed, J., Breeze, A. L., Overman, R., Phillips, C., and Norman, R. A. (2014) Structural insights into FGFR kinase isoform selectivity: diverse binding modes of AZD4547 and ponatinib in complex with FGFR1 and FGFR4 Structure 22, 1764-1774
    • (2014) Structure , vol.22 , pp. 1764-1774
    • Tucker, J.A.1    Klein, T.2    Breed, J.3    Breeze, A.L.4    Overman, R.5    Phillips, C.6    Norman, R.A.7
  • 35
    • 9744258219 scopus 로고    scopus 로고
    • Crystallography and the design of anti-AIDS drugs: Conformational flexibility and positional adaptability are important in the design of non-nucleoside HIV-1 reverse transcriptase inhibitors
    • Das, K., Lewi, P. J., Hughes, S. H., and Arnold, E. (2005) Crystallography and the design of anti-AIDS drugs: conformational flexibility and positional adaptability are important in the design of non-nucleoside HIV-1 reverse transcriptase inhibitors Prog. Biophys. Mol. Biol. 88, 209-231
    • (2005) Prog. Biophys. Mol. Biol. , vol.88 , pp. 209-231
    • Das, K.1    Lewi, P.J.2    Hughes, S.H.3    Arnold, E.4
  • 36
    • 77952724079 scopus 로고    scopus 로고
    • Crystal structures of HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278): Implications for drug design
    • Lansdon, E. B., Brendza, K. M., Hung, M., Wang, R., Mukund, S., Jin, D., Birkus, G., Kutty, N., and Liu, X. (2010) Crystal structures of HIV-1 reverse transcriptase with etravirine (TMC125) and rilpivirine (TMC278): implications for drug design J. Med. Chem. 53, 4295-4299
    • (2010) J. Med. Chem. , vol.53 , pp. 4295-4299
    • Lansdon, E.B.1    Brendza, K.M.2    Hung, M.3    Wang, R.4    Mukund, S.5    Jin, D.6    Birkus, G.7    Kutty, N.8    Liu, X.9
  • 37
    • 0030598848 scopus 로고    scopus 로고
    • Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism
    • Mohammadi, M., Schlessinger, J., and Hubbard, S. R. (1996) Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism Cell 86, 577-587
    • (1996) Cell , vol.86 , pp. 577-587
    • Mohammadi, M.1    Schlessinger, J.2    Hubbard, S.R.3
  • 38
    • 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. Sc.i USA 107, 2866-2871
    • (2010) Proc. Natl. Acad. Sc.I USA , 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
  • 39
    • 34548250374 scopus 로고    scopus 로고
    • A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases
    • Chen, H., Ma, J., Li, W., Eliseenkova, A. V., Xu, C., Neubert, T. A., Miller, W. T., and Mohammadi, M. (2007) A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases Mol. Cell 27, 717-730
    • (2007) Mol. Cell , vol.27 , pp. 717-730
    • Chen, H.1    Ma, J.2    Li, W.3    Eliseenkova, A.V.4    Xu, C.5    Neubert, T.A.6    Miller, W.T.7    Mohammadi, M.8
  • 40
    • 84860524795 scopus 로고    scopus 로고
    • Structural approaches to obtain kinase selectivity
    • Norman, R. A., Toader, D., and Ferguson, A. D. (2012) Structural approaches to obtain kinase selectivity Trends Pharmacol. Sci. 33, 273-278
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 273-278
    • Norman, R.A.1    Toader, D.2    Ferguson, A.D.3
  • 41
    • 84874340538 scopus 로고    scopus 로고
    • Structural insight into inactivation of plasminogen activator inhibitor-1 by a small-molecule antagonist
    • Lin, Z., Jensen, J. K., Hong, Z., Shi, X., Hu, L., Andreasen, P. A., and Huang, M. (2013) Structural insight into inactivation of plasminogen activator inhibitor-1 by a small-molecule antagonist Chem. Biol. 20, 253-261
    • (2013) Chem. Biol. , vol.20 , pp. 253-261
    • Lin, Z.1    Jensen, J.K.2    Hong, Z.3    Shi, X.4    Hu, L.5    Andreasen, P.A.6    Huang, M.7
  • 42
    • 53649083930 scopus 로고    scopus 로고
    • Small molecule recognition of c-Src via the Imatinib-binding conformation
    • Dar, A. C., Lopez, M. S., and Shokat, K. M. (2008) Small molecule recognition of c-Src via the Imatinib-binding conformation Chem. Biol. 15, 1015-1022
    • (2008) Chem. Biol. , vol.15 , pp. 1015-1022
    • Dar, A.C.1    Lopez, M.S.2    Shokat, K.M.3
  • 43
    • 84896353876 scopus 로고    scopus 로고
    • The free energy landscape in translational science: How can somatic mutations result in constitutive oncogenic activation?
    • Tsai, C. J. and Nussinov, R. (2014) The free energy landscape in translational science: how can somatic mutations result in constitutive oncogenic activation? Phys. Chem. Chem. Phys. 16, 6332-6341
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , pp. 6332-6341
    • Tsai, C.J.1    Nussinov, R.2
  • 44
    • 84879510153 scopus 로고    scopus 로고
    • Effects of oncogenic mutations on the conformational free-energy landscape of EGFR kinase
    • Sutto, L. and Gervasio, F. L. (2013) Effects of oncogenic mutations on the conformational free-energy landscape of EGFR kinase Proc. Natl. Acad. Sci. U.S.A. 110, 10616-10621
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 10616-10621
    • Sutto, L.1    Gervasio, F.L.2
  • 45
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: Evolution of dynamic regulatory proteins
    • Taylor, S. S. and Kornev, A. P. (2011) Protein kinases: evolution of dynamic regulatory proteins Trends Biochem. Sci. 36, 65-77
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 47
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang, J., Yang, P. L., and Gray, N. S. (2009) Targeting cancer with small molecule kinase inhibitors Nat. Rev. Cancer 9, 28-39
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 48
    • 38149088192 scopus 로고    scopus 로고
    • Flexible ligand-flexible protein docking in protein kinase systems
    • Wong, C. F. (2008) Flexible ligand-flexible protein docking in protein kinase systems Biochim. Biophys. Acta 1784, 244-251
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 244-251
    • Wong, C.F.1
  • 49
    • 75149130051 scopus 로고    scopus 로고
    • Targeting the cancer kinome through polypharmacology
    • Knight, Z. A., Lin, H., and Shokat, K. M. (2010) Targeting the cancer kinome through polypharmacology Nat. Rev. Cancer 10, 130-137
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 130-137
    • Knight, Z.A.1    Lin, H.2    Shokat, K.M.3
  • 50
    • 80755125565 scopus 로고    scopus 로고
    • Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity
    • Anastassiadis, T., Deacon, S. W., Devarajan, K., Ma, H., and Peterson, J. R. (2011) Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity Nat. Biotechnol. 29, 1039-1045
    • (2011) Nat. Biotechnol. , vol.29 , pp. 1039-1045
    • Anastassiadis, T.1    Deacon, S.W.2    Devarajan, K.3    Ma, H.4    Peterson, J.R.5
  • 51
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes
    • Minor, W., Cymborowski, M., Otwinowski, Z., and Chruszcz, M. (2006) HKL-3000: the integration of data reduction and structure solution - from diffraction images to an initial model in minutes Acta Crystallogr. D Biol. Crystallogr. 62, 859-866
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4


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