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Volumn 5, Issue 5, 2003, Pages 447-453

EGFR activation coupled to inhibition of tyrosine phosphatases causes lateral signal propagation

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; LIGAND; PROTEIN TYROSINE PHOSPHATASE; REACTIVE OXYGEN METABOLITE; TYROSINE KINASE RECEPTOR;

EID: 0038732770     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb981     Document Type: Article
Times cited : (200)

References (27)
  • 1
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 103, 211-225 (2000).
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 2
    • 0027303959 scopus 로고
    • Aggregation-induced activation of the epidermal growth factor receptor protein tyrosine kinase
    • Mohammadi, M. et al. Aggregation-induced activation of the epidermal growth factor receptor protein tyrosine kinase. Biochemistry 32, 8742-8748 (1993).
    • (1993) Biochemistry , vol.32 , pp. 8742-8748
    • Mohammadi, M.1
  • 3
    • 0023100261 scopus 로고
    • Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor
    • Yarden, Y. & Schlessinger, J. Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor. Biochemistry 26, 1443-1451 (1987).
    • (1987) Biochemistry , vol.26 , pp. 1443-1451
    • Yarden, Y.1    Schlessinger, J.2
  • 4
    • 0023848318 scopus 로고
    • Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent
    • Cochet, C. et al. 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).
    • (1988) J. Biol. Chem. , vol.263 , pp. 3290-3295
    • Cochet, C.1
  • 5
    • 0027320431 scopus 로고
    • Real-time measurements of kinetics of EGF binding to soluble EGF receptor monomers and dimers support the dimerization model for receptor activation
    • Zhou, M. et al. Real-time measurements of kinetics of EGF binding to soluble EGF receptor monomers and dimers support the dimerization model for receptor activation. Biochemistry 32, 8193-8198 (1993).
    • (1993) Biochemistry , vol.32 , pp. 8193-8198
    • Zhou, M.1
  • 6
    • 0023156382 scopus 로고
    • Self-phosphorylation of epidermal growth factor receptor: Evidence for a model of intermolecular allosteric activation
    • Yarden, Y. & Schlessinger, J. Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation. Biochemistry 26, 1434-1442 (1987).
    • (1987) Biochemistry , vol.26 , pp. 1434-1442
    • Yarden, Y.1    Schlessinger, J.2
  • 7
    • 0000317172 scopus 로고
    • Evidence that autophosphorylation of solubilized receptors for epidermal growth factor is mediated by intermolecular cross-phosphorylation
    • Honegger, A. M., Kris, R. M., Ullrich, A. & Schlessinger, J. Evidence that autophosphorylation of solubilized receptors for epidermal growth factor is mediated by intermolecular cross-phosphorylation. Proc. Natl Acad. Sci. USA 86, 925-929 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 925-929
    • Honegger, A.M.1    Kris, R.M.2    Ullrich, A.3    Schlessinger, J.4
  • 8
    • 0030795612 scopus 로고    scopus 로고
    • The ErbB signaling network in embryogenesis and oncogenesis: Signal diversification through combinatorial ligand-receptor interactions
    • Alroy, I. & Yarden, Y. The ErbB signaling network in embryogenesis and oncogenesis: signal diversification through combinatorial ligand-receptor interactions. FEBS Lett. 410, 83-86 (1997).
    • (1997) FEBS Lett. , vol.410 , pp. 83-86
    • Alroy, I.1    Yarden, Y.2
  • 9
    • 0024246872 scopus 로고
    • Non-catalytic domains of cytoplasmic protein-tyrosine kinases: Regulatory elements in signal transduction
    • Pawson, T. Non-catalytic domains of cytoplasmic protein-tyrosine kinases: regulatory elements in signal transduction. Oncogene 3, 491-495 (1988).
    • (1988) Oncogene , vol.3 , pp. 491-495
    • Pawson, T.1
  • 10
    • 0028596158 scopus 로고
    • An alternative to SH2 domains for binding tyrosine-phosphorylated proteins
    • Kavanaugh, W. M. & Williams, L. T. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 266, 1862-1865 (1994).
    • (1994) Science , vol.266 , pp. 1862-1865
    • Kavanaugh, W.M.1    Williams, L.T.2
  • 11
    • 0034711405 scopus 로고    scopus 로고
    • Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane
    • Verveer, P. J., Wouters, F. S., Reynolds, A. R. & Bastiaens, P. I. H. Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane. Science 290, 1567-1570 (2000).
    • (2000) Science , vol.290 , pp. 1567-1570
    • Verveer, P.J.1    Wouters, F.S.2    Reynolds, A.R.3    Bastiaens, P.I.H.4
  • 12
    • 0035371620 scopus 로고    scopus 로고
    • Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases
    • Ostman, A. & Bohmer, D. Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases. Trends Cell Biol. 11, 258-260 (2001).
    • (2001) Trends Cell Biol. , vol.11 , pp. 258-260
    • Ostman, A.1    Bohmer, D.2
  • 13
    • 0028843581 scopus 로고
    • Hydrogen peroxide preferentially enhances the tyrosine phosphorylation of epidermal growth factor receptor
    • Gamou, S. & Shimizu, N. Hydrogen peroxide preferentially enhances the tyrosine phosphorylation of epidermal growth factor receptor. FEBS Lett. 357, 161-164 (1995).
    • (1995) FEBS Lett. , vol.357 , pp. 161-164
    • Gamou, S.1    Shimizu, N.2
  • 14
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu, J. M. & Tanner, K. G. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37, 5633-5642 (1998).
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 15
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng, T. C., Fukada, T. & Tonks, N. K. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9, 387-399 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 16
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • Finkel, T. Oxygen radicals and signaling. Curr. Opin. Cell Biol. 10, 248-253 (1998).
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 248-253
    • Finkel, T.1
  • 17
    • 0030987181 scopus 로고    scopus 로고
    • A model for the activation of the epidermal growth factor receptor kinase involvement of an asymmetric dimer?
    • Groenen, L. C., Walker, F., Burgess, A. W. & Treutlein, H. R. A model for the activation of the epidermal growth factor receptor kinase involvement of an asymmetric dimer? Biochemistry 36, 3826-3836 (1997).
    • (1997) Biochemistry , vol.36 , pp. 3826-3836
    • Groenen, L.C.1    Walker, F.2    Burgess, A.W.3    Treutlein, H.R.4
  • 18
    • 0036532226 scopus 로고    scopus 로고
    • Self-perpetuating states in signal transduction positive feedback, double-negative feedback and bistability
    • Ferrell, J. E. Self-perpetuating states in signal transduction positive feedback, double-negative feedback and bistability. Curr. Opin. Cell Biol. 14, 140-148 (2002).
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 140-148
    • Ferrell, J.E.1
  • 21
    • 0032524350 scopus 로고    scopus 로고
    • Autoregulatory mechanisms in protein tyrosine kinases
    • Hubbard, S. R., Mohammadi, M. & Schlessinger, J. Autoregulatory mechanisms in protein tyrosine kinases. J. Biol. Chem. 273, 11987-11990 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 11987-11990
    • Hubbard, S.R.1    Mohammadi, M.2    Schlessinger, J.3
  • 22
    • 0022365046 scopus 로고
    • Self-phosphorylation enhances the protein-tyrosine kinase activity of the epidermal growth factor receptor
    • Bertics, P. J. & Gill, G. N. Self-phosphorylation enhances the protein-tyrosine kinase activity of the epidermal growth factor receptor. J. Biol. Chem. 260, 14642-14647 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 14642-14647
    • Bertics, P.J.1    Gill, G.N.2
  • 23
    • 0026056923 scopus 로고
    • Autophosphorylation of the intracellular domain of the epidermal growth factor receptor results in different effects on its tyrosine kinase activity with various peptide substrates
    • Hsu, C. Y., Hurwitz, D. R., Mervic, M. & Zilberstein, A. Autophosphorylation of the intracellular domain of the epidermal growth factor receptor results in different effects on its tyrosine kinase activity with various peptide substrates. J. Biol. Chem. 266, 603-608 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 603-608
    • Hsu, C.Y.1    Hurwitz, D.R.2    Mervic, M.3    Zilberstein, A.4
  • 24
    • 0026324171 scopus 로고
    • Protein tyrosine phosphatases: A diverse family of intracellular and transmembrane enzymes
    • Fischer, E. H., Charbonneau, H. & Tonks, N. K. Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes. Science 253, 401-406 (1991).
    • (1991) Science , vol.253 , pp. 401-406
    • Fischer, E.H.1    Charbonneau, H.2    Tonks, N.K.3
  • 25
    • 0036696824 scopus 로고    scopus 로고
    • Lateral propagation of EGF signalling after local stimulation is dependent on receptor density
    • Sawano, A., Takayama, S., Matsuda, M. & Miyawaki, A. Lateral propagation of EGF signalling after local stimulation is dependent on receptor density. Dev. Cell 3, 245-257 (2002).
    • (2002) Dev. Cell , vol.3 , pp. 245-257
    • Sawano, A.1    Takayama, S.2    Matsuda, M.3    Miyawaki, A.4
  • 26
    • 0032545445 scopus 로고    scopus 로고
    • Diphenyleneiodonium, an NAD(P)H oxidase inhibitor, also potently inhibits mitochondrial reactive oxygen species production
    • Li, Y. & Trush, M. A. Diphenyleneiodonium, an NAD(P)H oxidase inhibitor, also potently inhibits mitochondrial reactive oxygen species production. Biochem. Biophys. Res. Commun. 253, 295-299 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 295-299
    • Li, Y.1    Trush, M.A.2
  • 27
    • 0034029599 scopus 로고    scopus 로고
    • Global analysis of fluorescence lifetime imaging microscopy data
    • Verveer, P. J., Squire, A. & Bastiaens, P. I. H. Global analysis of fluorescence lifetime imaging microscopy data. Biophys. J. 78, 2127-2137 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 2127-2137
    • Verveer, P.J.1    Squire, A.2    Bastiaens, P.I.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.