메뉴 건너뛰기




Volumn 40, Issue 1, 2012, Pages 189-194

Investigating extracellular in situ EGFR structure and conformational changes using FRET microscopy

Author keywords

Crystallographic structure; Epidermal growth factor receptor signalling (EGFR signalling); Epidermal growth factor receptor structure (EGFR structure); ErbB; F rster resonance energy transfer imaging (FRET imaging); Molecular dynamics simulation

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR;

EID: 84856280574     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20110632     Document Type: Review
Times cited : (7)

References (50)
  • 1
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. (2000) Cell signaling by receptor tyrosine kinases. Cell 103, 211-225
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 3
    • 0021204118 scopus 로고
    • Autophosphorylation sites on the epidermal growth factor receptor
    • Downward, J., Parker, P. and Waterfield, M.D. (1984) Autophosphorylation sites on the epidermal growth factor receptor. Nature 311, 483-485 (Pubitemid 14035459)
    • (1984) Nature , vol.311 , Issue.5985 , pp. 483-485
    • Downward, J.1    Parker, P.2    Waterfield, M.D.3
  • 4
    • 33847718214 scopus 로고    scopus 로고
    • The EGF receptor family: spearheading a merger of signaling and therapeutics
    • DOI 10.1016/j.ceb.2007.02.008, PII S0955067407000221
    • Bublil, E.M. and Yarden, Y. (2007) The EGF receptor family: spearheading a merger of signaling and therapeutics. Curr. Opin. Cell Biol. 19, 124-134 (Pubitemid 46386405)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.2 , pp. 124-134
    • Bublil, E.M.1    Yarden, Y.2
  • 5
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: The complexity of targeted inhibitors
    • DOI 10.1038/nrc1609
    • Hynes, N.E. and Lane, H.A. (2005) ERBB receptors and cancer: the complexity of targeted inhibitors. Nat. Rev. Cancer 5, 341-354 (Pubitemid 40637826)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 6
    • 0021273420 scopus 로고
    • Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells
    • Ullrich, A., Coussens, L., Hayflick, J.S., Dull, T.J., Gray, A., Tam, A.W., Lee, J., Yarden, Y., Libermann, T.A., Schlessinger, J. et al. (1984) Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature 309, 418-425 (Pubitemid 14102443)
    • (1984) Nature , vol.309 , Issue.5967 , pp. 418-425
    • Ullrich, A.1    Coussens, L.2    Hayflick, J.S.3
  • 7
    • 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
  • 10
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • DOI 10.1016/S1097-2765(03)00047-9
    • Ferguson, K.M., Berger, M.B., Mendrola, J.M., Cho, H.S., Leahy, D.J. and Lemmon, M.A. (2003) EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol. Cell 11, 507-517 (Pubitemid 36297057)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.-S.4    Leahy, D.J.5    Lemmon, M.A.6
  • 12
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • Hyun-Soo, C. and Leahy, D.J. (2002) Structure of the extracellular region of HER3 reveals an interdomain tether. Science 297, 1330-1333
    • (2002) Science , vol.297 , pp. 1330-1333
    • Hyun-Soo, C.1    Leahy, D.J.2
  • 14
    • 18644386251 scopus 로고    scopus 로고
    • Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains
    • DOI 10.1016/S0092-8674(02)00963-7
    • Ogiso, H., Ishitani, R., Nureki, O., Fukai, S., Yamanaka, M., Kim, J.H., Saito, K., Sakamoto, A., Inoue, M., Shirouzu, M. and Yokoyama, S. (2002) Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell 110, 775-787 (Pubitemid 35291060)
    • (2002) Cell , vol.110 , Issue.6 , pp. 775-787
    • Ogiso, H.1    Ishitani, R.2    Nureki, O.3    Fukai, S.4    Yamanaka, M.5    Kim, J.-H.6    Saito, K.7    Sakamoto, A.8    Inoue, M.9    Shirouzu, M.10    Yokoyama, S.11
  • 15
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • Cho, H.S. and Leahy, D.J. (2002) Structure of the extracellular region of HER3 reveals an interdomain tether. Science 297, 1330-1333
    • (2002) Science , vol.297 , pp. 1330-1333
    • Cho, H.S.1    Leahy, D.J.2
  • 16
    • 0034638917 scopus 로고    scopus 로고
    • Overexpression of ErbB2 in cancer and ErbB2-targeting strategies
    • DOI 10.1038/sj.onc.1203972
    • Yu, D. and Hung, M.C. (2000) Overexpression of ErbB2 in cancer and ErbB2-targeting strategies. Oncogene 19, 6115-6121 (Pubitemid 32059461)
    • (2000) Oncogene , vol.19 , Issue.53 , pp. 6115-6121
    • Yu, D.1    Hung, M.-C.2
  • 17
    • 0029814271 scopus 로고    scopus 로고
    • A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor
    • Tzahar, E., Waterman, H., Chen, X., Levkowitz, G., Karunagaran, D., Lavi, S., Ratzkin, B.J. and Yarden, Y. (1996) A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor. Mol. Cell. Biol. 16, 5276-5287 (Pubitemid 26315047)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.10 , pp. 5276-5287
    • Tzahar, E.1    Waterman, H.2    Chen, X.3    Levkowitz, G.4    Karunagaran, D.5    Lavi, S.6    Ratzkin, B.J.7    Yarden, Y.8
  • 18
    • 33746905531 scopus 로고    scopus 로고
    • Phosphotyrosine interactome of the ErbB-receptor kinase family
    • Schulze, W.X., Deng, L. and Mann, M. (2005) Phosphotyrosine interactome of the ErbB-receptor kinase family. Mol. Syst. Biol. 1, 2005.0008
    • (2005) Mol. Syst. Biol. , vol.1
    • Schulze, W.X.1    Deng, L.2    Mann, M.3
  • 19
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: Towards the systems level
    • DOI 10.1038/nrm1962, PII NRM1962
    • Citri, A. and Yarden, Y. (2006) EGF-ERBB signalling: towards the systems level. Nat. Rev. Mol. Cell Biol. 7, 505-516 (Pubitemid 44036456)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 20
    • 0023156382 scopus 로고
    • Self-phosphorylation of epidermal growth factor receptor: Evidence for a model of intermolecular allosteric activation
    • DOI 10.1021/bi00379a034
    • Yarden, Y. and Schlessinger, J. (1987) Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation. Biochemistry 26, 1434-1442 (Pubitemid 17045874)
    • (1987) Biochemistry , vol.26 , Issue.5 , pp. 1434-1442
    • Yarden, Y.1    Schlessinger, J.2
  • 21
    • 0023100261 scopus 로고
    • Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor
    • DOI 10.1021/bi00379a035
    • Yarden, Y. and Schlessinger, J. (1987) Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor. Biochemistry 26, 1443-1451 (Pubitemid 17045875)
    • (1987) Biochemistry , vol.26 , Issue.5 , pp. 1443-1451
    • Yarden, Y.1    Schlessinger, J.2
  • 22
    • 0023848318 scopus 로고
    • Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent
    • Cochet, C., Kashles, O., Chambaz, E.M., Borrello, I., King, C.R. and Schlessinger, J. (1988) Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent. J. Biol. Chem. 263, 3290-3295 (Pubitemid 18072785)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.7 , pp. 3290-3295
    • Cochet, C.1    Kashles, O.2    Chambaz, E.M.3    Borrello, I.4    King, C.R.5    Schlessinger, J.6
  • 23
    • 0023930686 scopus 로고
    • Chicken epidermal growth factor (EGF) receptor: CDNA cloning, expression in mouse cells, and differential binding of EGF and transforming growth factor-α
    • Lax, I., Johnson, A., Howk, R., Sap, J., Bellot, F., Winkler, M., Ullrich, A., Vennstrom, B., Schlessinger, J. and Givol, D. (1988) Chicken epidermal growth factor (EGF) receptor: cDNA cloning, expression in mouse cells, and differential binding of EGF and transforming growth factor-α. Mol. Cell. Biol. 8, 1970-1978
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1970-1978
    • Lax, I.1    Johnson, A.2    Howk, R.3    Sap, J.4    Bellot, F.5    Winkler, M.6    Ullrich, A.7    Vennstrom, B.8    Schlessinger, J.9    Givol, D.10
  • 24
    • 0033544892 scopus 로고    scopus 로고
    • Dimerization of the extracellular domain of the receptor for epidermal growth factor containing the membrane-spanning segment in response to treatment with epidermal growth factor
    • Tanner, K.G. and Kyte, J. (1999) Dimerization of the extracellular domain of the receptor for epidermal growth factor containing the membrane-spanning segment in response to treatment with epidermal growth factor. J. Biol. Chem. 274, 35985-35990 (Pubitemid 129512909)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.50 , pp. 35985-35990
    • Tanner, K.G.1    Kyte, J.2
  • 25
    • 0025819768 scopus 로고
    • Rotational mobility of high-affinity epidermal growth factor receptors on the surface of living A431 cells
    • Zidovetzki, R., Johnson, D.A., Arndtjovin, D.J. and Jovin, T.M. (1991) Rotational mobility of high-affinity epidermal growth factor receptors on the surface of living A431 cells. Biochemistry 30, 6162-6166
    • (1991) Biochemistry , vol.30 , pp. 6162-6166
    • Zidovetzki, R.1    Johnson, D.A.2    Arndtjovin, D.J.3    Jovin, T.M.4
  • 26
    • 0000957072 scopus 로고    scopus 로고
    • Subnanosecond polarized microfluorimetry in the time domain: An instrument for studying receptor trafficking in live cells
    • Martin-Fernandez, M.L., Tobin, M.J., Clarke, D.T., Gregory, C.M. and Jones, G.R. (1998) Subnanosecond polarized microfluorimetry in the time domain: an instrument for studying receptor trafficking in live cells. Rev. Sci. Instrum. 69, 540-543 (Pubitemid 128599998)
    • (1998) Review of Scientific Instruments , vol.69 , Issue.1-2 , pp. 540-543
    • Martin-Fernandez, M.L.1    Tobin, M.J.2    Clarke, D.T.3    Gregory, C.M.4    Jones, G.R.5
  • 28
    • 0024841734 scopus 로고
    • Epidermal growth factor binding induces a conformation change in the external domain of its receptor
    • Greenfield, C., Hiles, I., Waterfield, M.D., Federwisch, M., Wollmer, A., Blundell, T.L. and McDonald, N. (1989) Epidermal growth factor binding induces a conformational change in the external domain of its receptor. EMBO J. 8, 4115-4123 (Pubitemid 20066854)
    • (1989) EMBO Journal , vol.8 , Issue.13 , pp. 4115-4123
    • Greenfield, C.1    Hiles, I.2    Waterfield, M.D.3    Federwisch, M.4    Wollmer, A.5    Blundell, T.L.6    McDonald, N.7
  • 29
    • 0025873538 scopus 로고
    • Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF receptor: A low resolution projection structure of the ligand-binding domain
    • Lax, I., Mitra, A.K., Ravera, C., Hurwitz, D.R., Rubinstein, M., Ullrich, A., Stroud, R.M. and Schlessinger, J. (1991) Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF receptor: a low resolution projection structure of the ligand-binding domain. J. Biol. Chem. 266, 13828-13833 (Pubitemid 21907427)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.21 , pp. 13828-13833
    • Lax, I.1    Mitra, A.K.2    Ravera, C.3    Hurwitz, D.R.4    Rubinstein, M.5    Ullrich, A.6    Stroud, R.M.7    Schlessinger, J.8
  • 30
    • 0023443196 scopus 로고
    • Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding
    • Bonischnetzler, M. and Pilch, P.F. (1987) Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding. Proc. Natl. Acad. Sci. U.S.A. 84, 7832-7836
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 7832-7836
    • Bonischnetzler, M.1    Pilch, P.F.2
  • 31
    • 0036320471 scopus 로고    scopus 로고
    • Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling
    • DOI 10.1091/mbc.01-08-0411
    • Yu, X.C., Sharma, K.D., Takahashi, T., Iwamoto, R. and Mekada, E. (2002) Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling. Mol. Biol. Cell 13, 2547-2557 (Pubitemid 34831354)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.7 , pp. 2547-2557
    • Yu, X.1    Sharma, K.D.2    Takahashi, T.3    Iwamoto, R.4    Mekada, E.5
  • 33
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy: A stereochemical model for tyrosine kinase receptor activation
    • Gadella, Jr, T.W. and Jovin, T.M. (1995) Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy: a stereochemical model for tyrosine kinase receptor activation. J. Cell. Biol. 129, 1543-1558
    • (1995) J. Cell. Biol. , vol.129 , pp. 1543-1558
    • Gadella Jr., T.W.1    Jovin, T.M.2
  • 34
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako, Y., Minoghchi, S. and Yanagida, T. (2000) Single-molecule imaging of EGFR signalling on the surface of living cells. Nat. Cell Biol. 2, 168-172
    • (2000) Nat. Cell Biol. , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 35
    • 0036225144 scopus 로고    scopus 로고
    • Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling
    • Martin-Fernandez, M., Clarke, D.T., Tobin, M.J., Jones, S.V. and Jones, G.R. (2002) Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling. Biophys. J. 82, 2415-2427 (Pubitemid 34441281)
    • (2002) Biophysical Journal , vol.82 , Issue.5 , pp. 2415-2427
    • Martin-Fernandez, M.1    Clarke, D.T.2    Tobin, M.J.3    Jones, S.V.4    Jones, G.R.5
  • 36
    • 0025775735 scopus 로고
    • Ligand-induced activation of A431 cell epidermal growth factor receptors occurs primarily by an autocrine pathway that acts upon receptors on the surface rather than intracellularly
    • Vandevijver, M.J., Kumar, R. and Mendelsohn, J. (1991) Ligand-induced activation of A431 cell epidermal growth factor receptors occurs primarily by an autocrine pathway that acts upon receptors on the surface rather than intracellularly. J. Biol. Chem. 266, 7503-7508 (Pubitemid 21906393)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.12 , pp. 7503-7508
    • Van De, V.M.J.1    Kumar, R.2    Mendelsohn, J.3
  • 37
    • 33748469013 scopus 로고    scopus 로고
    • Multidimensional single-molecule imaging in live cells using total-internal-reflection fluorescence microscopy
    • DOI 10.1364/OL.31.002157
    • Webb, S.E., Needham, S.R., Roberts, S.K. and Martin-Fernandez, M.L. (2006) Multidimensional single-molecule imaging in live cells using total-internal-reflection fluorescence microscopy. Opt. Lett. 31, 2157-2159 (Pubitemid 44542716)
    • (2006) Optics Letters , vol.31 , Issue.14 , pp. 2157-2159
    • Webb, S.E.D.1    Needham, S.R.2    Roberts, S.K.3    Martin-Fernandez, M.L.4
  • 39
    • 38549132873 scopus 로고    scopus 로고
    • Single-molecule imaging and fluorescence lifetime imaging microscopy show different structures for high- and low-affinity epidermal growth factor receptors in A431 cells
    • DOI 10.1529/biophysj.107.112623
    • Webb, S.E., Roberts, S.K., Needham, S.R., Tynan, C.J., Rolfe, D.J., Winn, M.D., Clarke, D.T., Barraclough, R. and Martin-Fernandez, M.L. (2008) Single-molecule imaging and fluorescence lifetime imaging microscopy show different structures for high- and low-affinity epidermal growth factor receptors in A431 cells. Biophys. J. 94, 803-819 (Pubitemid 351162449)
    • (2008) Biophysical Journal , vol.94 , Issue.3 , pp. 803-819
    • Webb, S.E.D.1    Roberts, S.K.2    Needham, S.R.3    Tynan, C.J.4    Rolfe, D.J.5    Winn, M.D.6    Clarke, D.T.7    Barraclough, R.8    Martin-Fernandez, M.L.9
  • 40
    • 24044436190 scopus 로고    scopus 로고
    • Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A multidimensional microscopy analysis
    • DOI 10.1074/jbc.M504770200
    • Clayton, A.H. A., Walker, F., Orchard, S.G., Henderson, C., Fuchs, D., Rothacker, J., Nice, E.C. and Burgess, A.W. (2005) Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor: a multidimensional microscopy analysis. J. Biol. Chem. 280, 30392-30399 (Pubitemid 41216222)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.34 , pp. 30392-30399
    • Clayton, A.H.A.1    Walker, F.2    Orchard, S.G.3    Henderson, C.4    Fuchs, D.5    Rothacker, J.6    Nice, E.C.7    Burgess, A.W.8
  • 41
    • 67649781716 scopus 로고    scopus 로고
    • Ectodomain orientation, conformational plasticity and oligomerization of ErbB1 receptors investigated by molecular dynamics
    • Kästner, J., Loeffler, H.H., Roberts, S.K., Martin-Fernandez, M.L. and Winn, M.D. (2009) Ectodomain orientation, conformational plasticity and oligomerization of ErbB1 receptors investigated by molecular dynamics. J. Struct. Biol. 167, 117-128
    • (2009) J. Struct. Biol. , vol.167 , pp. 117-128
    • Kästner, J.1    Loeffler, H.H.2    Roberts, S.K.3    Martin-Fernandez, M.L.4    Winn, M.D.5
  • 42
    • 0019121389 scopus 로고
    • Epidermal growth factor. Ability of tumor promoter to alter its degradation, receptor affinity and receptor number
    • Magun, B.E., Matrisian, L.M. and Bowden, G.T. (1980) Epidermal growth factor: ability of tumor promoter to alter its degradation, receptor affinity and receptor number. J. Biol. Chem. 255, 6373-6381 (Pubitemid 11229423)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.13 , pp. 6373-6381
    • Magun, B.E.1    Matrisian, L.M.2    Bowden, G.T.3
  • 43
    • 0018774782 scopus 로고
    • Biologically active phorbol esters specifically alter affinity of epidermal growth factor membrane receptors
    • DOI 10.1038/279387a0
    • Shoyab, M., Delarco, J.E. and Todaro, G.J. (1979) Biologically-active phorbol esters specifically alter affinity of epidermal growth factor membrane receptors. Nature 279, 387-391 (Pubitemid 9184714)
    • (1979) Nature , vol.279 , Issue.5712 , pp. 387-391
    • Shoyab, M.1    De Larco, J.E.2    Todaro, G.J.3
  • 47
    • 38349190632 scopus 로고    scopus 로고
    • Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system
    • Macdonald, J.L. and Pike, L.J. (2008) Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system. Proc. Natl. Acad. Sci. U.S.A. 105, 112-117
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 112-117
    • Macdonald, J.L.1    Pike, L.J.2
  • 48
    • 77955627615 scopus 로고    scopus 로고
    • Structural basis for negative cooperativity in growth factor binding to an EGF receptor
    • Alvarado, D., Klein, D.E. and Lemmon, M.A. (2010) Structural basis for negative cooperativity in growth factor binding to an EGF receptor. Cell 142, 568-579
    • (2010) Cell , vol.142 , pp. 568-579
    • Alvarado, D.1    Klein, D.E.2    Lemmon, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.