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Volumn 42, Issue 1, 2014, Pages 114-119

Structure-function relationships and supramolecular organization of the EGFR (epidermal growth factor receptor) on the cell surface

Author keywords

Cortical actin; Dimerization; Epidermal growth factor receptor (EGFR); Oligomerization; Single molecule localization

Indexed keywords

ACTIN; EPIDERMAL GROWTH FACTOR RECEPTOR;

EID: 84893273182     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20130236     Document Type: Article
Times cited : (17)

References (48)
  • 1
    • 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
  • 2
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • 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
    • (2003) Mol. Cell , vol.11 , 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
  • 3
    • 18644370411 scopus 로고    scopus 로고
    • Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor α
    • Garrett, T.P., McKern, N.M., Lou, M., Elleman, T.C., Adams, T.E., Lovrecz, G.O., Zhu, H.J., Walker, F., Frenkel, M.J., Hoyne, P.A. et al. (2002) Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor α. Cell 110, 763-773
    • (2002) Cell , vol.110 , pp. 763-773
    • Garrett, T.P.1    McKern, N.M.2    Lou, M.3    Elleman, T.C.4    Adams, T.E.5    Lovrecz, G.O.6    Zhu, H.J.7    Walker, F.8    Frenkel, M.J.9    Hoyne, P.A.10
  • 4
    • 34447313361 scopus 로고    scopus 로고
    • Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis
    • Saffarian, S., Li, Y., Elson, E.L. and Pike, L.J. (2007) Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis. Biophys. J. 93, 1021-1031
    • (2007) Biophys. J. , vol.93 , pp. 1021-1031
    • Saffarian, S.1    Li, Y.2    Elson, E.L.3    Pike, L.J.4
  • 5
    • 34447299688 scopus 로고    scopus 로고
    • Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy
    • Liu, P., Sudhaharan, T., Koh, R.M., Hwang, L.C., Ahmed, S., Maruyama, I.N. and Wohland, T. (2007) Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy. Biophys. J. 93, 684-698
    • (2007) Biophys. J. , vol.93 , pp. 684-698
    • Liu, P.1    Sudhaharan, T.2    Koh, R.M.3    Hwang, L.C.4    Ahmed, S.5    Maruyama, I.N.6    Wohland, T.7
  • 6
    • 34247230905 scopus 로고    scopus 로고
    • Unligated epidermal growth factor receptor forms higher order oligomers within microclusters on A431 cells that are sensitive to tyrosine kinase inhibitor binding
    • Clayton, A.H., Tavarnesi, M.L. and Johns, T.G. (2007) Unligated epidermal growth factor receptor forms higher order oligomers within microclusters on A431 cells that are sensitive to tyrosine kinase inhibitor binding. Biochemistry 46, 4589-4597
    • (2007) Biochemistry , vol.46 , pp. 4589-4597
    • Clayton, A.H.1    Tavarnesi, M.L.2    Johns, T.G.3
  • 7
    • 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
    • Clayton, A.H., 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
    • (2005) J. Biol. Chem. , vol.280 , pp. 30392-30399
    • Clayton, A.H.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
  • 8
    • 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
    • (2002) Biophys. J. , vol.82 , pp. 2415-2427
    • Martin-Fernandez, M.1    Clarke, D.T.2    Tobin, M.J.3    Jones, S.V.4    Jones, G.R.5
  • 9
    • 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
  • 13
    • 78049239930 scopus 로고    scopus 로고
    • Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis
    • Nagy, P., Claus, J., Jovin, T.M. and Arndt-Jovin, D.J. (2010) Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis. Proc. Natl. Acad. Sci. U.S.A. 107, 16524-16529
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 16524-16529
    • Nagy, P.1    Claus, J.2    Jovin, T.M.3    Arndt-Jovin, D.J.4
  • 16
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell, W.L., Cafiso, D.S. and Altenbach, C. (2000) Identifying conformational changes with site-directed spin labeling. Nat. Struct. Biol. 7, 735-739
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 17
    • 70349207749 scopus 로고    scopus 로고
    • Single-particle tracking methods for the study of membrane receptors dynamics
    • Alcor, D., Gouzer, G. and Triller, A. (2009) Single-particle tracking methods for the study of membrane receptors dynamics. Eur. J. Neurosci. 30, 987-997
    • (2009) Eur. J. Neurosci. , vol.30 , pp. 987-997
    • Alcor, D.1    Gouzer, G.2    Triller, A.3
  • 18
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust, M.J., Bates, M. and Zhuang, X. (2006) Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat. Methods 3, 793-795
    • (2006) Nat. Methods , vol.3 , pp. 793-795
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 20
    • 0028460042 scopus 로고
    • Breaking the diffraction resolution limit by stimulated emission: Stimulated-emission-depletion fluorescence microscopy
    • Hell, S.W. and Wichmann, J. (1994) Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy. Opt. Lett. 19, 780-782
    • (1994) Opt. Lett. , vol.19 , pp. 780-782
    • Hell, S.W.1    Wichmann, J.2
  • 21
    • 33746232609 scopus 로고
    • Near-field optical-scanning microscopy
    • Durig, U., Pohl, D.W. and Rohner, F. (1986) Near-field optical-scanning microscopy. J. Appl. Phys. 59, 3318-3327
    • (1986) J. Appl. Phys. , vol.59 , pp. 3318-3327
    • Durig, U.1    Pohl, D.W.2    Rohner, F.3
  • 22
    • 0037832404 scopus 로고    scopus 로고
    • Myosin v walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • Yildiz, A., Forkey, J.N., McKinney, S.A., Ha, T., Goldman, Y.E. and Selvin, P.R. (2003) Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization. Science 300, 2061-2065
    • (2003) Science , vol.300 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6
  • 23
    • 2342582682 scopus 로고    scopus 로고
    • Single-molecule high-resolution imaging with photobleaching
    • Gordon, M.P., Ha, T. and Selvin, P.R. (2004) Single-molecule high-resolution imaging with photobleaching. Proc. Natl. Acad. Sci. U.S.A. 101, 6462-6465
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 6462-6465
    • Gordon, M.P.1    Ha, T.2    Selvin, P.R.3
  • 24
    • 3843104585 scopus 로고    scopus 로고
    • Nanometer-localized multiple single-molecule fluorescence microscopy
    • Qu, X., Wu, D., Mets, L. and Scherer, N.F. (2004) Nanometer-localized multiple single-molecule fluorescence microscopy. Proc. Natl. Acad. Sci. U.S.A. 101, 11298-11303
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 11298-11303
    • Qu, X.1    Wu, D.2    Mets, L.3    Scherer, N.F.4
  • 25
    • 0034760118 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in cell biology
    • Axelrod, D. (2001) Total internal reflection fluorescence microscopy in cell biology. Traffic 2, 764-774
    • (2001) Traffic , vol.2 , pp. 764-774
    • Axelrod, D.1
  • 28
    • 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
    • (1999) J. Biol. Chem. , vol.274 , pp. 35985-35990
    • Tanner, K.G.1    Kyte, J.2
  • 29
    • 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
  • 30
    • 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
    • (1988) J. Biol. Chem. , vol.263 , pp. 3290-3295
    • Cochet, C.1    Kashles, O.2    Chambaz, E.M.3    Borrello, I.4    King, C.R.5    Schlessinger, J.6
  • 31
    • 0023100261 scopus 로고
    • Epidermal growth-factor induces rapid, reversible aggregation of the purified epidermal growth-factor receptor
    • Yarden, Y. and Schlessinger, J. (1987) Epidermal growth-factor induces rapid, reversible aggregation of the purified epidermal growth-factor receptor. Biochemistry 26, 1443-1451
    • (1987) Biochemistry , vol.26 , pp. 1443-1451
    • Yarden, Y.1    Schlessinger, J.2
  • 33
    • 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
    • (1991) J. Biol. Chem. , vol.266 , 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
  • 34
    • 0342965191 scopus 로고
    • Visualization by fluorescence of the binding and internalization of epidermal growth factor in human carcinoma cells A-431
    • Haigler, H., Ash, J.F., Singer, S.J. and Cohen, S. (1978) Visualization by fluorescence of the binding and internalization of epidermal growth factor in human carcinoma cells A-431. Proc. Natl. Acad. Sci. U.S.A. 75, 3317-3321
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 3317-3321
    • Haigler, H.1    Ash, J.F.2    Singer, S.J.3    Cohen, S.4
  • 35
    • 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
  • 36
    • 0036320471 scopus 로고    scopus 로고
    • Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling
    • 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
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2547-2557
    • Yu, X.C.1    Sharma, K.D.2    Takahashi, T.3    Iwamoto, R.4    Mekada, E.5
  • 37
    • 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
  • 38
    • 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
    • (1991) J. Biol. Chem. , vol.266 , pp. 7503-7508
    • Vandevijver, M.J.1    Kumar, R.2    Mendelsohn, J.3
  • 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
    • 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
    • (2008) Biophys. J. , vol.94 , pp. 803-819
    • Webb, S.E.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
  • 41
    • 67649781716 scopus 로고    scopus 로고
    • Ectodomain orientation, conformational plasticity and oligomerization of ErbB1 receptors investigated by molecular dynamics
    • Kastner, 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
    • Kastner, J.1    Loeffler, H.H.2    Roberts, S.K.3    Martin-Fernandez, M.L.4    Winn, M.D.5
  • 42
    • 57749186680 scopus 로고    scopus 로고
    • Receptor overexpression or inhibition alters cell surface dynamics of EGF-EGFR interaction: New insights from real-time single molecule analysis
    • Yu, C., Hale, J., Ritchie, K., Prasad, N.K. and Irudayaraj, J. (2009) Receptor overexpression or inhibition alters cell surface dynamics of EGF-EGFR interaction: new insights from real-time single molecule analysis. Biochem. Biophys. Res. Commun. 378, 376-382
    • (2009) Biochem. Biophys. Res. Commun. , vol.378 , pp. 376-382
    • Yu, C.1    Hale, J.2    Ritchie, K.3    Prasad, N.K.4    Irudayaraj, J.5
  • 43
    • 0028823802 scopus 로고
    • Neu differentiation factor activation of ErbB-3 and ErbB-4 is cell-specific and displays a differential requirement for ErbB-2
    • Beerli, R.R., Grausporta, D., Woodscook, K., Chen, X.M., Yarden, Y. and Hynes, N.E. (1995) Neu differentiation factor activation of ErbB-3 and ErbB-4 is cell-specific and displays a differential requirement for ErbB-2. Mol. Cell. Biol. 15, 6496-6505
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6496-6505
    • Beerli, R.R.1    Grausporta, D.2    Woodscook, K.3    Chen, X.M.4    Yarden, Y.5    Hynes, N.E.6
  • 47
    • 0345564815 scopus 로고    scopus 로고
    • Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin
    • Kwik, J., Boyle, S., Fooksman, D., Margolis, L., Sheetz, M.P. and Eddin, M. (2003) Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin. Proc. Natl. Acad. Sci. U.S.A. 100, 13964-13969
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 13964-13969
    • Kwik, J.1    Boyle, S.2    Fooksman, D.3    Margolis, L.4    Sheetz, M.P.5    Eddin, M.6


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