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Volumn 95, Issue 4, 2008, Pages 2086-2096

Quantitative characterization of the large-scale association of ErbB1 and ErbB2 by flow cytometric homo-FRET measurements

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; ERBB2IP PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 50349083489     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.108.133371     Document Type: Article
Times cited : (55)

References (46)
  • 1
    • 0018771484 scopus 로고
    • Local aggregation of hormone-receptor complexes is required for activation by epidermal growth factor
    • Schechter, Y., L. Hernaez, J. Schlessinger, and P. Cuatrecasas. 1979. Local aggregation of hormone-receptor complexes is required for activation by epidermal growth factor. Nature. 278:835-838.
    • (1979) Nature , vol.278 , pp. 835-838
    • Schechter, Y.1    Hernaez, L.2    Schlessinger, J.3    Cuatrecasas, P.4
  • 3
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: Towards the systems level
    • Citri, A., and Y. Yarden. 2006. EGF-ERBB signalling: towards the systems level. Nat. Rev. Mol. Cell Biol. 7:505-516.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 4
    • 0033367737 scopus 로고    scopus 로고
    • Nagy, P., A. Jenei, S. Damjanovich, T. M. Jovin, and J. Szöllocombining double acute accentsi. 1999. Complexity of signal transduction mediated by ErbB2: clues to the potential of receptor-targeted cancer therapy. Pathol. Oncol. Res. 5:255-271.
    • Nagy, P., A. Jenei, S. Damjanovich, T. M. Jovin, and J. Szöllocombining double acute accentsi. 1999. Complexity of signal transduction mediated by ErbB2: clues to the potential of receptor-targeted cancer therapy. Pathol. Oncol. Res. 5:255-271.
  • 6
    • 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., H. Waterman, X. Chen, G. Levkowitz, D. Karunagaran, S. Lavi, B. J. Ratzkin, and Y. Yarden. 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.
    • (1996) Mol. Cell. Biol , vol.16 , 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
  • 7
    • 0033605560 scopus 로고    scopus 로고
    • ErbB-2 amplification inhibits down-regulation and induces constitutive activation of both ErbB-2 and epidermal growth factor receptors
    • Worthylake, R., L. K. Opresko, and H. S. Wiley. 1999. ErbB-2 amplification inhibits down-regulation and induces constitutive activation of both ErbB-2 and epidermal growth factor receptors. J. Biol. Chem. 274:8865-8874.
    • (1999) J. Biol. Chem , vol.274 , pp. 8865-8874
    • Worthylake, R.1    Opresko, L.K.2    Wiley, H.S.3
  • 8
    • 0042307325 scopus 로고    scopus 로고
    • The ErbB2/ErbB3 heterodimer functions as an oncogenic unit: ErbB2 requires ErbB3 to drive breast tumor cell proliferation
    • Holbro, T., R. R. Beerli, F. Maurer, M. Koziczak, C. F. Barbas 3rd, and N. E. Hynes. 2003. The ErbB2/ErbB3 heterodimer functions as an oncogenic unit: ErbB2 requires ErbB3 to drive breast tumor cell proliferation. Proc. Natl. Acad. Sci. USA. 100:8933-8938.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8933-8938
    • Holbro, T.1    Beerli, R.R.2    Maurer, F.3    Koziczak, M.4    Barbas 3rd, C.F.5    Hynes, N.E.6
  • 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, T. W., Jr., and T. M. Jovin. 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
  • 11
    • 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., T. Sudhaharan, R. M. Koh, L. C. Hwang, S. Ahmed, I. N. Maruyama, and T. Wohland. 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
  • 12
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • Moriki, T., H. Maruyama, and I. N. Maruyama. 2001. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J. Mol. Biol. 311:1011-1026.
    • (2001) J. Mol. Biol , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 13
    • 41049104403 scopus 로고    scopus 로고
    • Studies of distribution, location and dynamic properties of EGFR on the cell surface measured by image correlation spectroscopy
    • Keating, E., A. Nohe, and N. O. Petersen. 2007. Studies of distribution, location and dynamic properties of EGFR on the cell surface measured by image correlation spectroscopy. Eur. Biophys. J. 37:469-481.
    • (2007) Eur. Biophys. J , vol.37 , pp. 469-481
    • Keating, E.1    Nohe, A.2    Petersen, N.O.3
  • 14
    • 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., S. K. Roberts, S. R. Needham, C. J. Tynan, D. J. Rolfe, M. D. Winn, D. T. Clarke, R. Barraclough, and M. L. Martin-Fernandez. 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
  • 15
    • 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., M. L. Tavarnesi, and T. G. Johns. 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
  • 16
    • 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., F. Walker, S. G. Orchard, C. Henderson, D. Fuchs, J. Rothacker, E. C. Nice, and A. W. Burgess. 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
  • 17
    • 14844329868 scopus 로고    scopus 로고
    • Oligomers of ERBB3 have two distinct interfaces that differ in their sensitivity to disruption by heregulin
    • Kani, K., C. M. Warren, C. S. Kaddis, J. A. Loo, and R. Landgraf. 2005. Oligomers of ERBB3 have two distinct interfaces that differ in their sensitivity to disruption by heregulin. J. Biol. Chem. 280:8238-8247.
    • (2005) J. Biol. Chem , vol.280 , pp. 8238-8247
    • Kani, K.1    Warren, C.M.2    Kaddis, C.S.3    Loo, J.A.4    Landgraf, R.5
  • 18
    • 0034713838 scopus 로고    scopus 로고
    • Heregulin reverses the oligomerization of HER3
    • Landgraf, R., and D. Eisenberg. 2000. Heregulin reverses the oligomerization of HER3. Biochemistry. 39:8503-8511.
    • (2000) Biochemistry , vol.39 , pp. 8503-8511
    • Landgraf, R.1    Eisenberg, D.2
  • 19
    • 0033014064 scopus 로고    scopus 로고
    • Nagy, P., A. Jenei, A. K. Kirsch, J. Szöllocombining double acute accentsi, S. Damjanovich, and T. M. Jovin. 1999. Activation-dependent clustering of the ErbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy. J. Cell Sci. 112:1733-1741.
    • Nagy, P., A. Jenei, A. K. Kirsch, J. Szöllocombining double acute accentsi, S. Damjanovich, and T. M. Jovin. 1999. Activation-dependent clustering of the ErbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy. J. Cell Sci. 112:1733-1741.
  • 20
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako, Y., S. Minoghchi, and T. Yanagida. 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
  • 21
    • 0024392570 scopus 로고
    • Rotational and translational diffusion in membranes measured by fluorescence and phosphorescence methods
    • Jovin, T. M., and W. L. Vaz. 1989. Rotational and translational diffusion in membranes measured by fluorescence and phosphorescence methods. Methods Enzymol. 172:471-513.
    • (1989) Methods Enzymol , vol.172 , pp. 471-513
    • Jovin, T.M.1    Vaz, W.L.2
  • 23
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma, P., R. Varma, R. C. Sarasij, I. K. Gousset, G. Krishnamoorthy, M. Rao, and S. Mayor. 2004. Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell. 116:577-589.
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Gousset, I.K.4    Krishnamoorthy, G.5    Rao, M.6    Mayor, S.7
  • 24
    • 29144533892 scopus 로고    scopus 로고
    • Use of Förster's resonance energy transfer microscopy to study lipid rafts
    • Rao, M., and S. Mayor. 2005. Use of Förster's resonance energy transfer microscopy to study lipid rafts. Biochim. Biophys. Acta. 1746:221-233.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 221-233
    • Rao, M.1    Mayor, S.2
  • 25
    • 0029117442 scopus 로고
    • Theory and application of fluorescence homotransfer to melittin oligomerization
    • Runnels, L. W., and S. F. Scarlata. 1995. Theory and application of fluorescence homotransfer to melittin oligomerization. Biophys. J. 69:1569-1583.
    • (1995) Biophys. J , vol.69 , pp. 1569-1583
    • Runnels, L.W.1    Scarlata, S.F.2
  • 26
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R., and S. Mayor. 1998. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature. 394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 27
    • 34247599842 scopus 로고    scopus 로고
    • Enumeration of oligomerization states of membrane proteins in living cells by homo-FRET spectroscopy and microscopy: Theory and application
    • Yeow, E. K., and A. H. Clayton. 2007. Enumeration of oligomerization states of membrane proteins in living cells by homo-FRET spectroscopy and microscopy: theory and application. Biophys. J. 92:3098-3104.
    • (2007) Biophys. J , vol.92 , pp. 3098-3104
    • Yeow, E.K.1    Clayton, A.H.2
  • 28
    • 1942425048 scopus 로고    scopus 로고
    • Red-edge anisotropy microscopy enables dynamic imaging of homo-FRET between green fluorescent proteins in cells
    • Squire, A., P. J. Verveer, O. Rocks, and P. I. Bastiaens. 2004. Red-edge anisotropy microscopy enables dynamic imaging of homo-FRET between green fluorescent proteins in cells. J. Struct. Biol. 147:62-69.
    • (2004) J. Struct. Biol , vol.147 , pp. 62-69
    • Squire, A.1    Verveer, P.J.2    Rocks, O.3    Bastiaens, P.I.4
  • 29
    • 0002195713 scopus 로고
    • Fluorescence polarization and energy transfer: Theory and application
    • M. Melamed, P. Mullaney, and M. Mendelsohn, editors. John Wiley & Sons, New York
    • Jovin, T. M. 1979. Fluorescence polarization and energy transfer: theory and application. In Flow Cytometry and Sorting. M. Melamed, P. Mullaney, and M. Mendelsohn, editors. John Wiley & Sons, New York. 137-165.
    • (1979) Flow Cytometry and Sorting , pp. 137-165
    • Jovin, T.M.1
  • 30
    • 3242784810 scopus 로고    scopus 로고
    • Szentesi, G., G. Horváth, I. Bori, G. Vámosi, J. Szöllocombining double acute accentsi, R. Gáspár, S. Damjanovich, A. Jenei, and L. Mátyus. 2004. Computer program for determining fluorescence resonance energy transfer efficiency from flow cytometric data on a cell-by-cell basis. Comput. Methods Programs Biomed. 75:201-211.
    • Szentesi, G., G. Horváth, I. Bori, G. Vámosi, J. Szöllocombining double acute accentsi, R. Gáspár, S. Damjanovich, A. Jenei, and L. Mátyus. 2004. Computer program for determining fluorescence resonance energy transfer efficiency from flow cytometric data on a cell-by-cell basis. Comput. Methods Programs Biomed. 75:201-211.
  • 31
    • 0036628631 scopus 로고    scopus 로고
    • Sebestyén, Z., P. Nagy, G. Horváth, G. Vámosi, R. Debets, J. W. Gratama, D. R. Alexander, and J. Szöllocombining double acute accentsi. 2002. Long wavelength fluorophores and cell-by-cell correction for autofluorescence significantly improves the accuracy of flow cytometric energy transfer measurements on a dual-laser benchtop flow cytometer. Cytometry. 48:124-135.
    • Sebestyén, Z., P. Nagy, G. Horváth, G. Vámosi, R. Debets, J. W. Gratama, D. R. Alexander, and J. Szöllocombining double acute accentsi. 2002. Long wavelength fluorophores and cell-by-cell correction for autofluorescence significantly improves the accuracy of flow cytometric energy transfer measurements on a dual-laser benchtop flow cytometer. Cytometry. 48:124-135.
  • 33
    • 0034255214 scopus 로고    scopus 로고
    • Detection of receptor clustering by flow cytometric fluorescence anisotropy measurements
    • Bene, L., M. J. Fulwyler, and S. Damjanovich. 2000. Detection of receptor clustering by flow cytometric fluorescence anisotropy measurements. Cytometry. 40:292-306.
    • (2000) Cytometry , vol.40 , pp. 292-306
    • Bene, L.1    Fulwyler, M.J.2    Damjanovich, S.3
  • 34
    • 21444436216 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of the antagonist- and partial agonist-occupied states of the cholecystokinin receptor
    • Harikumar, K. G., and L. J. Miller. 2005. Fluorescence resonance energy transfer analysis of the antagonist- and partial agonist-occupied states of the cholecystokinin receptor. J. Biol. Chem. 280:18631-18635.
    • (2005) J. Biol. Chem , vol.280 , pp. 18631-18635
    • Harikumar, K.G.1    Miller, L.J.2
  • 35
    • 19444380683 scopus 로고    scopus 로고
    • Horváth, G., M. Petrás, G. Szentesi, A. Fábián, J. W. Park, G. Vereb, and J. Szöllocombining double acute accentsi. 2005. Selecting the right fluorophores and flow cytometer for fluorescence resonance energy transfer measurements. Cytometry A. 65:148-157.
    • Horváth, G., M. Petrás, G. Szentesi, A. Fábián, J. W. Park, G. Vereb, and J. Szöllocombining double acute accentsi. 2005. Selecting the right fluorophores and flow cytometer for fluorescence resonance energy transfer measurements. Cytometry A. 65:148-157.
  • 36
    • 23844475901 scopus 로고    scopus 로고
    • Mocanu, M. M., Z. Fazekas, M. Petrás, P. Nagy, Z. Sebestyén, J. Isola, J. Timar, J. W. Park, G. Vereb, and J. Szöllocombining double acute accentsi. 2005. Associations of ErbB2, beta1-integrin and lipid rafts on Herceptin (trastuzumab) resistant and sensitive tumor cell lines. Cancer Lett. 227:201-212.
    • Mocanu, M. M., Z. Fazekas, M. Petrás, P. Nagy, Z. Sebestyén, J. Isola, J. Timar, J. W. Park, G. Vereb, and J. Szöllocombining double acute accentsi. 2005. Associations of ErbB2, beta1-integrin and lipid rafts on Herceptin (trastuzumab) resistant and sensitive tumor cell lines. Cancer Lett. 227:201-212.
  • 37
    • 0037446068 scopus 로고    scopus 로고
    • Small interfering RNAs suppress the expression of endogenous and GFP-fused epidermal growth factor receptor (ErbB1) and induce apoptosis in ErbB1-overexpressing cells
    • Nagy, P., D. J. Arndt-Jovin, and T. M. Jovin. 2003. Small interfering RNAs suppress the expression of endogenous and GFP-fused epidermal growth factor receptor (ErbB1) and induce apoptosis in ErbB1-overexpressing cells. Exp. Cell Res. 285:39-49.
    • (2003) Exp. Cell Res , vol.285 , pp. 39-49
    • Nagy, P.1    Arndt-Jovin, D.J.2    Jovin, T.M.3
  • 38
    • 20444362337 scopus 로고    scopus 로고
    • Bene, L., J. Szöllocombining double acute accentsi, G. Szentesi, L. Damjanovich, R. Gáspár, Jr., T. A. Waldmann, and S. Damjanovich. 2005. Detection of receptor trimers on the cell surface by flow cytometric fluorescence energy homotransfer measurements. Biochim. Biophys. Acta. 1744:176-198.
    • Bene, L., J. Szöllocombining double acute accentsi, G. Szentesi, L. Damjanovich, R. Gáspár, Jr., T. A. Waldmann, and S. Damjanovich. 2005. Detection of receptor trimers on the cell surface by flow cytometric fluorescence energy homotransfer measurements. Biochim. Biophys. Acta. 1744:176-198.
  • 40
    • 0032101894 scopus 로고    scopus 로고
    • Nagy, P., L. Bene, M. Balázs, W. C. Hyun, S. J. Lockett, N. Y. Chiang, F. Waldman, B. G. Feuerstein, S. Damjanovich, and J. Szöllocombining double acute accentsi. 1998. EGF-induced redistribution of ErbB2 on breast tumor cells: flow and image cytometric energy transfer measurements. Cytometry. 32:120-131.
    • Nagy, P., L. Bene, M. Balázs, W. C. Hyun, S. J. Lockett, N. Y. Chiang, F. Waldman, B. G. Feuerstein, S. Damjanovich, and J. Szöllocombining double acute accentsi. 1998. EGF-induced redistribution of ErbB2 on breast tumor cells: flow and image cytometric energy transfer measurements. Cytometry. 32:120-131.
  • 46
    • 0037429779 scopus 로고    scopus 로고
    • The deaf and the dumb: The biology of ErbB-2 and ErbB-3
    • Citri, A., K. B. Skaria, and Y. Yarden. 2003. The deaf and the dumb: the biology of ErbB-2 and ErbB-3. Exp. Cell Res. 284:54-65.
    • (2003) Exp. Cell Res , vol.284 , pp. 54-65
    • Citri, A.1    Skaria, K.B.2    Yarden, Y.3


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