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Volumn 109, Issue 1, 2012, Pages 137-142

Mechanics of EGF receptor/ErbB2 kinase activation revealed by luciferase fragment complementation imaging

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; FIREFLY LUCIFERASE; HETERODIMER;

EID: 84855999013     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1111316109     Document Type: Article
Times cited : (59)

References (28)
  • 1
    • 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
  • 2
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: The complexity of targeted inhibitors
    • DOI 10.1038/nrc1609
    • Hynes NE, Lane HA (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
  • 3
    • 48249158391 scopus 로고    scopus 로고
    • Structure-based view of epidermal growth factor receptor regulation
    • Ferguson KM (2008) Structure-based view of epidermal growth factor receptor regulation. Annu Rev Biophys 37:353-373.
    • (2008) Annu Rev Biophys , vol.37 , pp. 353-373
    • Ferguson, K.M.1
  • 4
    • 63049100044 scopus 로고    scopus 로고
    • Functional selectivity of EGF family peptide growth factors: Implications for cancer
    • Wilson KJ, et al. (2009) Functional selectivity of EGF family peptide growth factors: Implications for cancer. Pharmacol Ther 122:1-8.
    • (2009) Pharmacol Ther , vol.122 , pp. 1-8
    • Wilson, K.J.1
  • 6
    • 0033608993 scopus 로고    scopus 로고
    • The ErbB2/HER2 oncoprotein of human carcinomas may function solely as a shared coreceptor for multiple stroma-derive growth factors
    • Klapper LN (1999) The ErbB2/HER2 oncoprotein of human carcinomas may function solely as a shared coreceptor for multiple stroma-derive growth factors. Proc Natl Acad Sci USA 96:4995-5000.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4995-5000
    • Klapper, L.N.1
  • 7
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
    • DOI 10.1093/emboj/16.7.1647
    • Graus Porta D, Beerli RR, Daly JM, Hynes NE (1997) ErbB2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling. EMBO J 16:1647-1655. (Pubitemid 27151960)
    • (1997) EMBO Journal , vol.16 , Issue.7 , pp. 1647-1655
    • Graus-Porta, D.1    Beerli, R.R.2    Daly, J.M.3    Hynes, N.E.4
  • 9
    • 67449146917 scopus 로고    scopus 로고
    • The juxtamembrane region of the EGF receptor functions as an activation domain
    • Brewer MR, et al. (2009) The juxtamembrane region of the EGF receptor functions as an activation domain. Mol Cell 34:641-651.
    • (2009) Mol Cell , vol.34 , pp. 641-651
    • Brewer, M.R.1
  • 10
    • 67549145398 scopus 로고    scopus 로고
    • Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment
    • Jura N, et al. (2009) Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment. Cell 137:1293-1307.
    • (2009) Cell , vol.137 , pp. 1293-1307
    • Jura, N.1
  • 11
    • 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, et al. (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
  • 12
    • 0029029617 scopus 로고
    • Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
    • Jeffrey PD, et al. (1995) Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376:313-320.
    • (1995) Nature , vol.376 , pp. 313-320
    • Jeffrey, P.D.1
  • 13
    • 77951248565 scopus 로고    scopus 로고
    • Her4 and Her2/neu tyrosine kinase domains dimerize and activate in a reconstituted in vitro system
    • Monsey J, Shen W, Schlesinger P, Bose R (2010) Her4 and Her2/neu tyrosine kinase domains dimerize and activate in a reconstituted in vitro system. J Biol Chem 285:7035-7044.
    • (2010) J Biol Chem , vol.285 , pp. 7035-7044
    • Monsey, J.1    Shen, W.2    Schlesinger, P.3    Bose, R.4
  • 14
    • 65549138069 scopus 로고    scopus 로고
    • Luciferase fragment complementation imaging of conformational changes in the EGF receptor
    • Yang KS, Ilagan MXG, Piwnica-Worms D, Pike LJ (2009) Luciferase fragment complementation imaging of conformational changes in the EGF receptor. J Biol Chem 284:7474-7482.
    • (2009) J Biol Chem , vol.284 , pp. 7474-7482
    • Yang, K.S.1    Ilagan, M.X.G.2    Piwnica-Worms, D.3    Pike, L.J.4
  • 15
    • 77954900212 scopus 로고    scopus 로고
    • Asp-960/Glu-961 Control the movement of the C-terminal tail of the EGF receptor to regulate asymmetric dimer formation
    • Yang KS, Macdonald-Obermann JL, Piwnica-Worms D, Pike LJ (2010) Asp-960/Glu-961 Control the movement of the C-terminal tail of the EGF receptor to regulate asymmetric dimer formation. J Biol Chem 285:24014-24022.
    • (2010) J Biol Chem , vol.285 , pp. 24014-24022
    • Yang, K.S.1    Macdonald-Obermann, J.L.2    Piwnica-Worms, D.3    Pike, L.J.4
  • 17
    • 0036225144 scopus 로고    scopus 로고
    • Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling
    • Martin-Fernandez M, et al. (2002) Preformed oligomeric epidermal growth factor receptors undergo and 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
  • 18
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako Y, Minoguchi S, 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    Minoguchi, S.2    Yanagida, T.3
  • 19
    • 55449102296 scopus 로고    scopus 로고
    • All EGF (ErbB) receptors have preformed homo- And heterodimeric structures in living cells
    • Tao R-H, Maruyama IN (2008) All EGF (ErbB) receptors have preformed homo- and heterodimeric structures in living cells. J Cell Sci 121:3207-3217.
    • (2008) J Cell Sci , vol.121 , pp. 3207-3217
    • Tao, R.-H.1    Maruyama, I.N.2
  • 20
    • 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, et al. (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
  • 22
    • 35348813658 scopus 로고    scopus 로고
    • Current state of imaging protein-protein interactions in vivo with genetically encoded reporters
    • DOI 10.1146/annurev.bioeng.9.060906.152044
    • Villalobos VM, Naik S, Piwnica-Worms D (2007) Current state of imaging protein-protein interactions in vivo with genetically encoded reporters. Annu Rev Biomed Eng 9:321-349. (Pubitemid 350246660)
    • (2007) Annual Review of Biomedical Engineering , vol.9 , pp. 321-349
    • Villalobos, V.1    Naik, S.2    Piwnica-Worms, D.3
  • 23
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
    • DOI 10.1074/jbc.M207135200
    • Stamos J, Sliwkowski MX, Eigenbrot C (2002) Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J Biol Chem 277:46265-46272. (Pubitemid 35417619)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.48 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 24
    • 84455161571 scopus 로고    scopus 로고
    • The membrane-proximal intracellular domain of the EGF receptor underlies negative cooperativity in ligand binding
    • 10.1074/jbc.M111.274175
    • Adak S, Yang KS, Macdonald-Obermann JL, Pike LJ (2011) The membrane-proximal intracellular domain of the EGF receptor underlies negative cooperativity in ligand binding. J Biol Chem, 10.1074/jbc.M111.274175.
    • (2011) J Biol Chem
    • Adak, S.1    Yang, K.S.2    Macdonald-Obermann, J.L.3    Pike, L.J.4
  • 25
    • 0028168569 scopus 로고
    • Insect cell-expressed p180ErbB3 possesses an impaired tyrosine kinase activity
    • Guy PM, et al. (1994) Insect cell-expressed p180ErbB3 possesses an impaired tyrosine kinase activity. Proc Natl Acad Sci USA 91:8132-8136.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8132-8136
    • Guy, P.M.1
  • 26
    • 77952338791 scopus 로고    scopus 로고
    • ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation
    • Shi F, et al. (2010) ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation. Proc Natl Acad Sci USA 107:7692-7697.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 7692-7697
    • Shi, F.1
  • 27
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • DOI 10.1006/jmbi.2001.4923
    • Moriki T, Maruyama H, Maruyama IN (2001) Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J Mol Biol 311:1011-1026. (Pubitemid 32803717)
    • (2001) Journal of Molecular Biology , vol.311 , Issue.5 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 28
    • 34447313361 scopus 로고    scopus 로고
    • Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis
    • DOI 10.1529/biophysj.107.105494
    • Saffarian S, Li Y, Elson EL, Pike LJ (2007) Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis. Biophys J 93:1021-1031. (Pubitemid 47219793)
    • (2007) Biophysical Journal , vol.93 , Issue.3 , pp. 1021-1031
    • Saffarian, S.1    Li, Y.2    Elson, E.L.3    Pikey, L.J.4


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