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Volumn 109, Issue 35, 2012, Pages 13984-13989

Dynamically varying interactions between heregulin and ErbB proteins detected by single-molecule analysis in living cells

Author keywords

Cell signaling; Epidermal growth factors; Ligand receptor interaction

Indexed keywords

DIMER; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 3; EPIDERMAL GROWTH FACTOR RECEPTOR 4; FLUORESCENT DYE; LIGAND; MONOMER; NEU DIFFERENTIATION FACTOR; RECEPTOR;

EID: 84865553091     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1200464109     Document Type: Article
Times cited : (40)

References (38)
  • 1
    • 0034600849 scopus 로고    scopus 로고
    • The ErbB signaling network: Receptor heterodimerization in development and cancer
    • Olayioye MA, Neve RM, Lane HA, Hynes NE (2000) The ErbB signaling network: Receptor heterodimerization in development and cancer. EMBO J 19:3159-3167. (Pubitemid 30428195)
    • (2000) EMBO Journal , vol.19 , Issue.13 , pp. 3159-3167
    • Olayioye, M.A.1    Neve, R.M.2    Lane, H.A.3    Hynes, N.E.4
  • 3
    • 0031936410 scopus 로고    scopus 로고
    • Specificity within the EGF family/ErbB receptor family signaling network
    • Riese DJ, II, Stern DF (1998) Specificity within the EGF family/ErbB receptor family signaling network. Bioessays 20:41-48.
    • (1998) Bioessays , vol.20 , pp. 41-48
    • Riese II, D.J.1    Stern, D.F.2
  • 4
    • 0037429722 scopus 로고    scopus 로고
    • ErbB-4: Mechanism of action and biology
    • Carpenter G (2003) ErbB-4: Mechanism of action and biology. Exp Cell Res 284:66-77.
    • (2003) Exp Cell Res , vol.284 , pp. 66-77
    • Carpenter, G.1
  • 6
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, 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
  • 7
    • 62649159075 scopus 로고    scopus 로고
    • Ligand-induced ErbB receptor dimerization
    • Lemmon MA (2009) Ligand-induced ErbB receptor dimerization. Exp Cell Res 315:638-648.
    • (2009) Exp Cell Res , vol.315 , pp. 638-648
    • Lemmon, M.A.1
  • 8
    • 0028358856 scopus 로고
    • Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin
    • Sliwkowski MX, et al. (1994) Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. J Biol Chem 269:14661-14665.
    • (1994) J Biol Chem , vol.269 , pp. 14661-14665
    • Sliwkowski, M.X.1
  • 9
    • 0029118223 scopus 로고
    • The cellular response to neuregulins is governed by complex interactions of the erbB receptor family
    • Riese DJ, van Raaij TM, Plowman GD, Adrews GC, Stern DF (1995) The cellular response to neuregulins is governed by complex interactions of the erbB receptor family. Mol Cell Biol 15:5770-5776.
    • (1995) Mol Cell Biol , vol.15 , pp. 5770-5776
    • Riese, D.J.1    Van Raaij, T.M.2    Plowman, G.D.3    Adrews, G.C.4    Stern, D.F.5
  • 10
    • 0034282556 scopus 로고    scopus 로고
    • Extracellular domains drive homo- But not hetero-dimerization of erbB receptors
    • Ferguson KM, Darling PJ, Mohan MJ, Macatee TL, Lemmon MA (2000) Extracellular domains drive homo- but not hetero-dimerization of erbB receptors. EMBO J 29:4632-4643.
    • (2000) EMBO J , vol.29 , pp. 4632-4643
    • Ferguson, K.M.1    Darling, P.J.2    Mohan, M.J.3    Macatee, T.L.4    Lemmon, M.A.5
  • 11
    • 0034713838 scopus 로고    scopus 로고
    • Heregulin reverses the oligomerization of HER3
    • DOI 10.1021/bi000953+
    • Landgraf R, Eisenberg D (2000) Heregulin reverses the oligomerization of HER3. Biochemistry 39:8503-8511. (Pubitemid 30489947)
    • (2000) Biochemistry , vol.39 , Issue.29 , pp. 8503-8511
    • Landgraf, R.1    Eisenberg, D.2
  • 13
    • 3042800393 scopus 로고    scopus 로고
    • ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface
    • DOI 10.1016/j.febslet.2004.06.014, PII S0014579304007343
    • Berger MB, Mendrola JM, Lemmon MA (2004) ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface. FEBS Lett 569:332-336. (Pubitemid 38849407)
    • (2004) FEBS Letters , vol.569 , Issue.1-3 , pp. 332-336
    • Berger, M.B.1    Mendrola, J.M.2    Lemmon, M.A.3
  • 14
    • 14844329868 scopus 로고    scopus 로고
    • Oligomers of ERBB3 have two distinct interfaces that differ in their sensitivity to disruption by heregulin
    • DOI 10.1074/jbc.M410944200
    • Kani K, Warren CM, Kaddis CS, Loo JA, Landgraf R (2005) Oligomers of ERBB3 have two distinct interfaces that differ in their sensitivity to disruption by heregulin. J Biol Chem 280:8238-8247. (Pubitemid 40349725)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 8238-8247
    • Kani, K.1    Warren, C.M.2    Kaddis, C.S.3    Loo, J.A.4    Landgraf, R.5
  • 18
    • 84857072115 scopus 로고    scopus 로고
    • Live cell single-molecule detection in systems biology
    • Sako Y, et al. (2011) Live cell single-molecule detection in systems biology. WIREs Systems Biol Med 4:183-192.
    • (2011) WIREs Systems Biol Med , vol.4 , pp. 183-192
    • Sako, Y.1
  • 19
    • 33748939242 scopus 로고    scopus 로고
    • Single-molecule analysis of epidermal growth factor binding on the surface of living cells
    • DOI 10.1038/sj.emboj.7601308, PII 7601308
    • Teramura Y, et al. (2006) Single-molecule analysis of epidermal growth factor binding on the surface of living cells. EMBO J 25:4215-4222. (Pubitemid 44435219)
    • (2006) EMBO Journal , vol.25 , Issue.18 , pp. 4215-4222
    • Teramura, Y.1    Ichinose, J.2    Takagi, H.3    Nishida, K.4    Yanagida, T.5    Sako, Y.6
  • 20
    • 0018774782 scopus 로고
    • Biologically active phorbol esters specifically alter affinity of epidermal growth factor membrane receptors
    • DOI 10.1038/279387a0
    • Shoyab M, De Larco JE, Todaro GJ (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
  • 21
    • 0019121389 scopus 로고
    • Epidermal growth factor. Ability of tumor promoter to alter its degradation, receptor affinity and receptor number
    • Magun BE, Matrisian LM, Bowden GT (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
  • 22
    • 38349190632 scopus 로고    scopus 로고
    • Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system
    • Macdonald JL, Pike LJ (2008) Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system. Proc Natl Acad Sci USA 105:112-117.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 112-117
    • Macdonald, J.L.1    Pike, L.J.2
  • 23
    • 78651399024 scopus 로고    scopus 로고
    • The tethering arm of the EGF receptor is required for negative cooperativity and signal transduction
    • Adak S, DeAndrade D, Pike LJ (2011) The tethering arm of the EGF receptor is required for negative cooperativity and signal transduction. J Biol Chem 286:1545-1555.
    • (2011) J Biol Chem , vol.286 , pp. 1545-1555
    • Adak, S.1    DeAndrade, D.2    Pike, L.J.3
  • 24
    • 77955627615 scopus 로고    scopus 로고
    • Structural basis for negative cooperativity in growth factor binding to an EGF receptor
    • Alvarado D, Klein DE, Lemmon MA (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
  • 25
    • 20444409504 scopus 로고    scopus 로고
    • Heterogeneities in EGF receptor density at the cell surface can lead to concave up scatchard plot of EGF binding
    • DOI 10.1016/j.febslet.2005.04.059, PII S0014579305005363
    • Mayawala K, Vlachos DG, Edwards JS (2005) Heterogeneities in EGF receptor density at the cell surface can lead to concave up scatchard plot of EGF binding. FEBS Lett 579:3043-3047. (Pubitemid 40797832)
    • (2005) FEBS Letters , vol.579 , Issue.14 , pp. 3043-3047
    • Mayawala, K.1    Vlachos, D.G.2    Edwards, J.S.3
  • 28
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • Cho HS, Leahy DJ (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
  • 29
    • 74449093106 scopus 로고    scopus 로고
    • Reversible dimerization of EGFR revealed by single-molecule fluorescence imaging using quantum dots
    • Kawashima N, et al. (2010) Reversible dimerization of EGFR revealed by single-molecule fluorescence imaging using quantum dots. Chem Eur J 16:1186-1192.
    • (2010) Chem Eur J , vol.16 , pp. 1186-1192
    • Kawashima, N.1
  • 30
    • 77950460037 scopus 로고    scopus 로고
    • Spatial control of EGF receptor activation by reversible dimerization on living cells
    • Chung I, et al. (2010) Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 464:783-787.
    • (2010) Nature , vol.464 , pp. 783-787
    • Chung, I.1
  • 31
    • 0026708050 scopus 로고
    • Implications of epidermal growth factor (EGF) induced EGF receptor aggregation
    • Wofsy C, Goldstein B, Lund K, Wiley HS (1992) Implications of epidermal growth factor (EGF) induced EGF receptor aggregation. Biophys J 63:98-110.
    • (1992) Biophys J , vol.63 , pp. 98-110
    • Wofsy, C.1    Goldstein, B.2    Lund, K.3    Wiley, H.S.4
  • 32
    • 78649814933 scopus 로고    scopus 로고
    • Ligand-induced EGF receptor oligomerization is kinase-dependent and enhances internalization
    • Hofman EG, et al. (2010) Ligand-induced EGF receptor oligomerization is kinase-dependent and enhances internalization. J Biol Chem 285:39481-39489.
    • (2010) J Biol Chem , vol.285 , pp. 39481-39489
    • Hofman, E.G.1
  • 33
    • 17844375949 scopus 로고    scopus 로고
    • Single-molecule analysis of epidermal growth factor signaling that leads to ultrasensitive calcium response
    • DOI 10.1529/biophysj.104.053330
    • Uyemura T, Takagi H, Yanagida T, Sako Y (2005) Single-molecule analysis of epidermal growth factor signaling that leads to ultrasensitive calcium response. Biophys J 88:3720-3730. (Pubitemid 40586619)
    • (2005) Biophysical Journal , vol.88 , Issue.5 , pp. 3720-3730
    • Uyemura, T.1    Takagi, H.2    Yanagida, T.3    Sako, Y.4
  • 34
    • 3042699999 scopus 로고    scopus 로고
    • Prolonged extracellular signal-regulated kinase 1/2 activation during fibroblast growth factor 1- of heregulin β1-induced antiestrogen-resistant growth of breast cancer cells is resistant to mitogen-activated protein/extracellular regulated kinase kinase inhibitors
    • DOI 10.1158/0008-5472.CAN-03-2645
    • Thottassery JV, et al. (2004) Prolonged extracellular signal-regulated kinase 1/2 activation during fibroblast growth factor 1- or heregulin β1-induced antiestrogen-resistant growth of breast cancer cells is resistant to mitogen-activated protein/extracellular regulated kinase kinase inhibitors. Cancer Res 64:4637-4647. (Pubitemid 38856938)
    • (2004) Cancer Research , vol.64 , Issue.13 , pp. 4637-4647
    • Thottassery, J.V.1    Sun, Y.2    Westbrook, L.3    Rentz, S.S.4    Manuvakhova, M.5    Qu, Z.6    Samuel, S.7    Upshaw, R.8    Cunningham, A.9    Kern, F.G.10
  • 35
    • 67649391241 scopus 로고    scopus 로고
    • The intracellular juxtamembrane domain of the epidermal growth factor (EGF) receptor is responsible for the allosteric regulation of EGF binding
    • Macdonald-Obermann JL, Pike LJ (2009) The intracellular juxtamembrane domain of the epidermal growth factor (EGF) receptor is responsible for the allosteric regulation of EGF binding. J Biol Chem 284:13570-13576.
    • (2009) J Biol Chem , vol.284 , pp. 13570-13576
    • Macdonald-Obermann, J.L.1    Pike, L.J.2
  • 37
    • 0032504049 scopus 로고    scopus 로고
    • Formation of a high affinity heregulin binding site using the soluble extracellular domains of ErbB2 with ErbB3 or ErbB4
    • DOI 10.1016/S0014-5793(98)00737-6, PII S0014579398007376
    • Fitzpatrick VD, Pisacane PI, Vandlen RL, Sliwkowski MX (1998) Formation of a high affinity heregulin binding site using the soluble extracellular domains of ErbB2 with ErbB3 or ErbB4. FEBS Lett 431:102-106. (Pubitemid 28330861)
    • (1998) FEBS Letters , vol.431 , Issue.1 , pp. 102-106
    • Fitzpatrick, V.D.1    Pisacane, P.I.2    Vandlen, R.L.3    Sliwkowski, M.X.4
  • 38
    • 73449090455 scopus 로고    scopus 로고
    • Learning rates and states from biophysical time series: A Bayesian approach to model selection and single-molecule FRET data
    • Bronson JE, Fei J, Hofman JM, Gonzalez RL, Wiggins CH (2009) Learning rates and states from biophysical time series: A Bayesian approach to model selection and single-molecule FRET data. Biophys J 97:3196-3205.
    • (2009) Biophys J , vol.97 , pp. 3196-3205
    • Bronson, J.E.1    Fei, J.2    Hofman, J.M.3    Gonzalez, R.L.4    Wiggins, C.H.5


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