메뉴 건너뛰기




Volumn 17, Issue 12, 1998, Pages 3385-3397

Differential endocytic routing of homo- and hetero-dimeric ErbB tyrosine kinases confers signaling superiority to receptor heterodimers

Author keywords

Endocytosis; ErbB; HER family; Oncogene; Signal transduction; Transforming growth factor

Indexed keywords

EPIDERMAL GROWTH FACTOR; PROTEIN TYROSINE KINASE; TRANSFORMING GROWTH FACTOR ALPHA;

EID: 0032526729     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.12.3385     Document Type: Article
Times cited : (351)

References (81)
  • 1
    • 0029053716 scopus 로고
    • Cooperative signaling of ErbB-3 and ErbB-2 in neoplastic transformation of human mammary carcinoma cells
    • Alimandi, M., Romano, A., Curia, M.C., Muraro, R., Fedi, P., Aaronson, S.A., Di Fiore, P.P. and Kraus, M.H. (1995) Cooperative signaling of ErbB-3 and ErbB-2 in neoplastic transformation of human mammary carcinoma cells. Oncogene, 15, 1813-1821.
    • (1995) Oncogene , vol.15 , pp. 1813-1821
    • Alimandi, M.1    Romano, A.2    Curia, M.C.3    Muraro, R.4    Fedi, P.5    Aaronson, S.A.6    Di Fiore, P.P.7    Kraus, M.H.8
  • 2
    • 0030795612 scopus 로고    scopus 로고
    • The ErbB signaling network in embryogenesis and oncogenesis: Signal diversification through combinatorial ligand-receptor interactions
    • Alroy, I. and Yarden, Y. (1997) The ErbB signaling network in embryogenesis and oncogenesis: signal diversification through combinatorial ligand-receptor interactions. FEBS Lett., 410, 83-86.
    • (1997) FEBS Lett. , vol.410 , pp. 83-86
    • Alroy, I.1    Yarden, Y.2
  • 3
    • 0022485548 scopus 로고
    • Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185
    • Bargmann, C.I., Hung, M.C. and Weinberg, R.A. (1986) Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of p185. Cell, 45, 649-657.
    • (1986) Cell , vol.45 , pp. 649-657
    • Bargmann, C.I.1    Hung, M.C.2    Weinberg, R.A.3
  • 4
    • 0023624729 scopus 로고
    • Cell migration is essential for sustained growth of keratinocyte colonies: The roles of transforming growth factor-α and epidermal growth factor
    • Barrandon, Y. and Green, H. (1987) Cell migration is essential for sustained growth of keratinocyte colonies: the roles of transforming growth factor-α and epidermal growth factor. Cell, 50, 1131-1137.
    • (1987) Cell , vol.50 , pp. 1131-1137
    • Barrandon, Y.1    Green, H.2
  • 5
    • 0019427474 scopus 로고
    • Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts
    • Basu, S.K., Goldstein, J.L., Anderson, R.G.W. and Brown, M.S. (1981) Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts. Cell, 24, 493-502.
    • (1981) Cell , vol.24 , pp. 493-502
    • Basu, S.K.1    Goldstein, J.L.2    Anderson, R.G.W.3    Brown, M.S.4
  • 6
    • 0029912203 scopus 로고    scopus 로고
    • All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired
    • Baulida, J., Kraus, M.H., Alimandi, M., Di Fiore, P.P. and Carpenter, G. (1996) All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired. J. Biol. Chem., 271, 5251-5257.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5251-5257
    • Baulida, J.1    Kraus, M.H.2    Alimandi, M.3    Di Fiore, P.P.4    Carpenter, G.5
  • 7
    • 0029965411 scopus 로고    scopus 로고
    • Epidermal growth factor-related peptides activate distinct subsets of ErbB receptors and differ in their biological activities
    • Beerli, R.R. and Hynes, N.E. (1996) Epidermal growth factor-related peptides activate distinct subsets of ErbB receptors and differ in their biological activities. J. Biol. Chem., 271, 6071-6076.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6071-6076
    • Beerli, R.R.1    Hynes, N.E.2
  • 8
    • 0028229715 scopus 로고
    • A single autophosphorylation site confers oncogenicity to the Neu/ErbB-2 receptor and enables coupling to the MAP-kinase pathway
    • Ben-Levy, R., Paterson, H.E. Marshall, C.J. and Yarden, Y. (1994) A single autophosphorylation site confers oncogenicity to the Neu/ErbB-2 receptor and enables coupling to the MAP-kinase pathway. EMBO J., 13, 3302-3311.
    • (1994) EMBO J. , vol.13 , pp. 3302-3311
    • Ben-Levy, R.1    Paterson, H.E.2    Marshall, C.J.3    Yarden, Y.4
  • 9
    • 0030919509 scopus 로고    scopus 로고
    • Neuregulins and their receptors: A versatile signaling module in organogenesis and oncogenesis
    • Burden, S. and Yarden, Y. (1997) Neuregulins and their receptors: a versatile signaling module in organogenesis and oncogenesis. Neuron, 18, 847-855.
    • (1997) Neuron , vol.18 , pp. 847-855
    • Burden, S.1    Yarden, Y.2
  • 10
    • 0024978029 scopus 로고
    • Role of acidic intracellular compartment in the biosynthesis of dictiostelium lysosomal enzymes
    • Cardelli, J.A., Richardson, J. and Meiars, D. (1989) Role of acidic intracellular compartment in the biosynthesis of dictiostelium lysosomal enzymes. J. Biol. Chem., 264, 3454-3464.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3454-3464
    • Cardelli, J.A.1    Richardson, J.2    Meiars, D.3
  • 11
    • 0028176477 scopus 로고
    • A neu acquaintance for ErbB3 and ErbB4: A role for receptor heterodimerization in growth signaling
    • Carraway, K.L. and Cantley, L.C. (1994) A neu acquaintance for ErbB3 and ErbB4: A role for receptor heterodimerization in growth signaling. Cell, 78, 5-8.
    • (1994) Cell , vol.78 , pp. 5-8
    • Carraway, K.L.1    Cantley, L.C.2
  • 12
    • 0029884288 scopus 로고    scopus 로고
    • Insulin regulates heregulin binding and ErbB3 expression in rat hepatocytes
    • Carver, R.S., Sliwkowski, M.X., Sitaric, S. and Russell, W.E. (1996) Insulin regulates heregulin binding and ErbB3 expression in rat hepatocytes. J. Biol. Chem., 271, 13491-13496.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13491-13496
    • Carver, R.S.1    Sliwkowski, M.X.2    Sitaric, S.3    Russell, W.E.4
  • 13
    • 0029804204 scopus 로고    scopus 로고
    • The relationship between human epidermal growth-like factor receptor expression and cellular transformation in NIH-3T3 cells
    • Cohen, B.D., Kiener, P.K., Green, J.M., Foy, L., Fell, H.P. and Zhang, K. (1996) The relationship between human epidermal growth-like factor receptor expression and cellular transformation in NIH-3T3 cells. J. Biol. Chem., 271, 30897-30903.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30897-30903
    • Cohen, B.D.1    Kiener, P.K.2    Green, J.M.3    Foy, L.4    Fell, H.P.5    Zhang, K.6
  • 15
    • 0027422247 scopus 로고
    • The pathway to signal achievement
    • Eagan, S.E. and Weinberg, R.A. (1993) The pathway to signal achievement. Nature, 365, 781-783.
    • (1993) Nature , vol.365 , pp. 781-783
    • Eagan, S.E.1    Weinberg, R.A.2
  • 16
    • 14844349947 scopus 로고
    • Epidermal growth factor and transforming growth factor-α: Differential intracellular routing and processing of ligand-receptor complexes
    • Ebner, R. and Derynck, R. (1991) Epidermal growth factor and transforming growth factor-α: differential intracellular routing and processing of ligand-receptor complexes. Cell Regul., 2, 599-612.
    • (1991) Cell Regul. , vol.2 , pp. 599-612
    • Ebner, R.1    Derynck, R.2
  • 17
    • 0025359062 scopus 로고
    • Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body
    • Felder, S., Miller, K., Moehren, G., Ullrich, A., Schlessinger, J. and Hopkins, C.R. (1990) Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body. Cell, 61, 623-634.
    • (1990) Cell , vol.61 , pp. 623-634
    • Felder, S.1    Miller, K.2    Moehren, G.3    Ullrich, A.4    Schlessinger, J.5    Hopkins, C.R.6
  • 18
    • 0024230493 scopus 로고
    • Rapid constitutive internalization and externalization of epidermal growth factor receptors in isolated rat hepatocytes
    • Gladhaug, I.P. and Christofferson, T. (1988) Rapid constitutive internalization and externalization of epidermal growth factor receptors in isolated rat hepatocytes. J. Biol. Chem., 263, 12199-12203.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12199-12203
    • Gladhaug, I.P.1    Christofferson, T.2
  • 19
    • 0023840804 scopus 로고
    • Ligand-induced endocytosis of the EGF receptor is blocked by mutational inactivation and by microinjection of anti-phosphotyrosine antibodies
    • Glenney, J.R., Chen, W.S., Lazar, C.S., Walton, G.M., Zokas, L.M., Rosenfeld, M.G. and Gill, G.N. (1988) Ligand-induced endocytosis of the EGF receptor is blocked by mutational inactivation and by microinjection of anti-phosphotyrosine antibodies. Cell, 52, 675-684.
    • (1988) Cell , vol.52 , pp. 675-684
    • Glenney, J.R.1    Chen, W.S.2    Lazar, C.S.3    Walton, G.M.4    Zokas, L.M.5    Rosenfeld, M.G.6    Gill, G.N.7
  • 20
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
    • Graus-Porta, D., Beerly, R., Daly, J.M. and Hynes, N.E. (1997) ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling. EMBO J., 16, 1647-1655.
    • (1997) EMBO J. , vol.16 , pp. 1647-1655
    • Graus-Porta, D.1    Beerly, R.2    Daly, J.M.3    Hynes, N.E.4
  • 21
    • 0020538097 scopus 로고
    • Demonstration of permanent factor-dependent multipotential (erythroid/neutrophil/basophil) hematopoietic progenitor cell lines
    • Greenberger, J.S., Sakakeeny, M.A., Humphries, R.K., Eaves, C.J. and Eckner, R.J. (1983) Demonstration of permanent factor-dependent multipotential (erythroid/neutrophil/basophil) hematopoietic progenitor cell lines. Proc. Natl Acad. Sci. USA, 80, 2931-2935.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 2931-2935
    • Greenberger, J.S.1    Sakakeeny, M.A.2    Humphries, R.K.3    Eaves, C.J.4    Eckner, R.J.5
  • 22
    • 0030783917 scopus 로고    scopus 로고
    • Reduced ability of transforming growth factor-α to induce EGF receptor heterodimerization and downregulation suggests a mechanism of oncogenic synergy with ErbB2
    • Gulliford, T.J., Huang, G.C., Ouyang, X. and Epstein, E.J. (1997) Reduced ability of transforming growth factor-α to induce EGF receptor heterodimerization and downregulation suggests a mechanism of oncogenic synergy with ErbB2. Oncogene, 15, 2219-2223.
    • (1997) Oncogene , vol.15 , pp. 2219-2223
    • Gulliford, T.J.1    Huang, G.C.2    Ouyang, X.3    Epstein, E.J.4
  • 23
    • 0029914718 scopus 로고    scopus 로고
    • Epidermal growth factor behaves as a partial agonist in hepatocytes: Effects on DNA synthesis in primary culture and competition with transforming growth factor α
    • Guren, T.K., Thoresen, G.H., Dajani, O.F., Taraldsrud, E., Moberg, E.R. and Christoffersen, T. (1996) Epidermal growth factor behaves as a partial agonist in hepatocytes: effects on DNA synthesis in primary culture and competition with transforming growth factor α. Growth Factors, 13, 171-179.
    • (1996) Growth Factors , vol.13 , pp. 171-179
    • Guren, T.K.1    Thoresen, G.H.2    Dajani, O.F.3    Taraldsrud, E.4    Moberg, E.R.5    Christoffersen, T.6
  • 27
    • 0023430930 scopus 로고
    • Increased expression of the putative growth factor receptor p185HER-2 causes transformation and tumorigenesis of NIH-3T3
    • Hudziak, R.M. Schlessinger, J. and Ullrich, A. (1987) Increased expression of the putative growth factor receptor p185HER-2 causes transformation and tumorigenesis of NIH-3T3. Proc. Natl Acad. Sci. USA, 84, 7159-7163.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7159-7163
    • Hudziak, R.M.1    Schlessinger, J.2    Ullrich, A.3
  • 28
    • 0028670125 scopus 로고
    • The biology of erbB-2/neu/HER-2 and its role in cancer
    • Hynes, N.E. and Stern, D.F. (1994) The biology of erbB-2/neu/HER-2 and its role in cancer. Biochem. Biophys. Acta, 1198, 165-184.
    • (1994) Biochem. Biophys. Acta , vol.1198 , pp. 165-184
    • Hynes, N.E.1    Stern, D.F.2
  • 29
    • 0023872192 scopus 로고
    • Establishment of mouse cell lines that constitutively secrete large quantities of interleukins 2, 3, 4 or 5, using modified cDNA expression vectors
    • Karasuyama, H. and Melchers, F. (1988) Establishment of mouse cell lines that constitutively secrete large quantities of interleukins 2, 3, 4 or 5, using modified cDNA expression vectors. Eur. J. Immunol., 18, 97-104.
    • (1988) Eur. J. Immunol. , vol.18 , pp. 97-104
    • Karasuyama, H.1    Melchers, F.2
  • 31
    • 0028077047 scopus 로고
    • Epidermal growth factor-dependent association of phosphatidylinositol 3′-kinase with the erbB-3 gene product
    • Kim, H.-H., Sierke, S.L. and Koland, J.G. (1994) Epidermal growth factor-dependent association of phosphatidylinositol 3′-kinase with the erbB-3 gene product. J. Biol. Chem., 269, 24747-24755.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24747-24755
    • Kim, H.-H.1    Sierke, S.L.2    Koland, J.G.3
  • 32
    • 0030959114 scopus 로고    scopus 로고
    • A subclass of tumor-inhibitory monoclonal antibodies to erbB-2/HER2 blocks crosstalk with growth factor receptors
    • Klapper, L.N., Vaisman, N., Hurwitz, E., Pinkas-Kramarski, R., Yarden, Y. and Sela, M. (1997) A subclass of tumor-inhibitory monoclonal antibodies to erbB-2/HER2 blocks crosstalk with growth factor receptors. Oncogene, 14, 2099-2109.
    • (1997) Oncogene , vol.14 , pp. 2099-2109
    • Klapper, L.N.1    Vaisman, N.2    Hurwitz, E.3    Pinkas-Kramarski, R.4    Yarden, Y.5    Sela, M.6
  • 33
    • 0025765803 scopus 로고
    • SH-2 and SH-3 domains: Elements that control interactions of cytoplasmic signaling proteins
    • Koch, A.C. Anderson, D., Moran, M.F., Ellis, C. and Pawson, T. (1991) SH-2 and SH-3 domains: Elements that control interactions of cytoplasmic signaling proteins. Science, 252, 668-674.
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, A.C.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 34
    • 0024395587 scopus 로고
    • Synergistic interaction of p185c-neu and the EGF receptor leads to transformation of rodent fibroblasts
    • Kokai, Y. Myers, J.N., Wada, T., Brown, V.I., LeVea, C.M., Davis, J.G., Dobashi, K. and Greene, M.I. (1989) Synergistic interaction of p185c-neu and the EGF receptor leads to transformation of rodent fibroblasts. Cell 58, 287-292.
    • (1989) Cell , vol.58 , pp. 287-292
    • Kokai, Y.1    Myers, J.N.2    Wada, T.3    Brown, V.I.4    LeVea, C.M.5    Davis, J.G.6    Dobashi, K.7    Greene, M.I.8
  • 35
    • 0024435665 scopus 로고
    • Attenuated processing of epidermal growth factor in the face of marked degradation of transforming growth factor α
    • Korc, M. and Finman, J.E. (1989) Attenuated processing of epidermal growth factor in the face of marked degradation of transforming growth factor α. J. Biol. Chem., 264, 14990-14999.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14990-14999
    • Korc, M.1    Finman, J.E.2
  • 36
    • 0031081140 scopus 로고    scopus 로고
    • Vulval development in Caenorhabditis elegans
    • Kornfeld, K. (1997) Vulval development in Caenorhabditis elegans. Trends Genet., 13, 55-61.
    • (1997) Trends Genet. , vol.13 , pp. 55-61
    • Kornfeld, K.1
  • 37
    • 0028245026 scopus 로고
    • Identification of the high affinity binding site of transforming growth factor-α (TGF-α) for the chicken epidermal growth factor (EGF) receptor using EGF/TGF-α chimeras
    • Kramer, R.H., Leferink, A.E.G., van Buern-Koornneef, I.L., van der Meer, A., van de Poll, M.L.M. and van Zoelen, E.J.J. (1994) Identification of the high affinity binding site of transforming growth factor-α (TGF-α) for the chicken epidermal growth factor (EGF) receptor using EGF/TGF-α chimeras. J. Biol. Chem., 269, 8708-8711.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8708-8711
    • Kramer, R.H.1    Leferink, A.E.G.2    Van Buern-Koornneef, I.L.3    Van Der Meer, A.4    Van De Poll, M.L.M.5    Van Zoelen, E.J.J.6
  • 38
    • 0028884413 scopus 로고
    • Requirement for neuregulin receptor erbB2 in neural and cardiac development
    • Lee, K.F., Simon, H., Chen, H., Bates, B., Hung, M.C. and Hauser, C. (1995) Requirement for neuregulin receptor erbB2 in neural and cardiac development. Nature, 378, 394-398.
    • (1995) Nature , vol.378 , pp. 394-398
    • Lee, K.F.1    Simon, H.2    Chen, H.3    Bates, B.4    Hung, M.C.5    Hauser, C.6
  • 39
    • 0030663020 scopus 로고    scopus 로고
    • Superagonistic behaviour of epidermal growth factor/transforming growth factor-α chimeras: Correlation with receptor routing after ligand-induced internalization
    • Lenferink, A.E.G., Kramer, R.H., van Vugt, M.J.H., Konigswieser, M., di-Fiore, P.P., van Zoelen, E.J.J. and van de Poll, L.M.L. (1997) Superagonistic behaviour of epidermal growth factor/transforming growth factor-α chimeras: correlation with receptor routing after ligand-induced internalization. Biochem. J., 327, 859-865.
    • (1997) Biochem. J. , vol.327 , pp. 859-865
    • Lenferink, A.E.G.1    Kramer, R.H.2    Van Vugt, M.J.H.3    Konigswieser, M.4    Di-Fiore, P.P.5    Van Zoelen, E.J.J.6    Van De Poll, L.M.L.7
  • 40
    • 0029917264 scopus 로고    scopus 로고
    • Coupling of the c-Cbl protooncogene product to ErbB-1/EGF-receptor but not to other ErbB proteins
    • Levkowitz, G., Klapper, L.N., Tzahar, E., Freywald, A., Sela, M. and Yarden, Y. (1996) Coupling of the c-Cbl protooncogene product to ErbB-1/EGF-receptor but not to other ErbB proteins. Oncogene, 12, 1117-1125.
    • (1996) Oncogene , vol.12 , pp. 1117-1125
    • Levkowitz, G.1    Klapper, L.N.2    Tzahar, E.3    Freywald, A.4    Sela, M.5    Yarden, Y.6
  • 41
    • 0029740245 scopus 로고    scopus 로고
    • A comparison of epidermal growth factor receptor-mediated mitogenic signaling in response to transforming growth factor α and epidermal growth factor in cultured fetal rat hepatocytes
    • Lipeski, L.E., Boylan, J.M. and Gruppuso, P.A. (1996) A comparison of epidermal growth factor receptor-mediated mitogenic signaling in response to transforming growth factor α and epidermal growth factor in cultured fetal rat hepatocytes. Biochem. Mol. Biol. Int., 39, 975-983.
    • (1996) Biochem. Mol. Biol. Int. , vol.39 , pp. 975-983
    • Lipeski, L.E.1    Boylan, J.M.2    Gruppuso, P.A.3
  • 42
    • 0025687686 scopus 로고
    • The normal erbB-2 product is an atypical receptor-like tyrosine kinase with constitutive activity in the absence of ligand
    • Lonardo, F., Di Marco, E., King, C.R., Pierce, J.H., Segatto, O., Aaronson, S.A. and Di Fiore, P.P. (1990) The normal erbB-2 product is an atypical receptor-like tyrosine kinase with constitutive activity in the absence of ligand. New Biol., 2, 992-1003.
    • (1990) New Biol. , vol.2 , pp. 992-1003
    • Lonardo, F.1    Di Marco, E.2    King, C.R.3    Pierce, J.H.4    Segatto, O.5    Aaronson, S.A.6    Di Fiore, P.P.7
  • 43
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall, C.J. (1995) Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell, 80, 179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 44
    • 0021399556 scopus 로고
    • Biosynthesis of the epidermal growth factor receptor in A431 cels
    • Mayes, E.L.V. and Waterfield, M.D. (1984) Biosynthesis of the epidermal growth factor receptor in A431 cels. EMBO J., 3, 531-537.
    • (1984) EMBO J. , vol.3 , pp. 531-537
    • Mayes, E.L.V.1    Waterfield, M.D.2
  • 46
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosman, T. (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods, 65, 55-63.
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosman, T.1
  • 47
    • 0025362617 scopus 로고
    • Fusions of Staphylococal protein A
    • Nilson, B. and Abrahmsen, L. (1990) Fusions of Staphylococal protein A. Methods Enymol., 185, 144-161.
    • (1990) Methods Enymol. , vol.185 , pp. 144-161
    • Nilson, B.1    Abrahmsen, L.2
  • 48
    • 0027465159 scopus 로고
    • Cell-type specific interaction of Neu differentiation factor (NDF/heregulin) with Neu/HER-2 suggests complex ligand-receptor relationships
    • Peles, E., Ben-Levy, R., Tzahar, E., Liu, N., Wen, D. and Yarden, Y. (1993) Cell-type specific interaction of Neu differentiation factor (NDF/heregulin) with Neu/HER-2 suggests complex ligand-receptor relationships. EMBO J., 12, 961-971.
    • (1993) EMBO J. , vol.12 , pp. 961-971
    • Peles, E.1    Ben-Levy, R.2    Tzahar, E.3    Liu, N.4    Wen, D.5    Yarden, Y.6
  • 50
    • 0029783549 scopus 로고    scopus 로고
    • Neu differentiation factor/neuregulin isoforms activate distinct receptor combinations
    • Pinkas-Kramarski, R., Shelly, M., Glathe, S., Ratzkin, B.J. and Yarden, Y. (1996b) Neu differentiation factor/neuregulin isoforms activate distinct receptor combinations. J. Biol. Chem., 271, 19029-19032.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19029-19032
    • Pinkas-Kramarski, R.1    Shelly, M.2    Glathe, S.3    Ratzkin, B.J.4    Yarden, Y.5
  • 51
    • 0029850715 scopus 로고    scopus 로고
    • The interaction of an epidermal growth factor/transforming growth factor α tail chimera with the human epidermal growth factor receptor reveals unexpected complexities
    • Puddicombe, S.M., Wood, L., Chamberlin, S.G. and Davies, D. (1996) The interaction of an epidermal growth factor/transforming growth factor α tail chimera with the human epidermal growth factor receptor reveals unexpected complexities. J. Biol. Chem., 271, 30392-30397.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30392-30397
    • Puddicombe, S.M.1    Wood, L.2    Chamberlin, S.G.3    Davies, D.4
  • 53
    • 0029976245 scopus 로고    scopus 로고
    • Receptor-mediated effects of ligand availability influence relative mitogenic potencies of epidermal growth factor and transforming growth factor α
    • Reddy, C.C., Wells, A. and Laffenburger, D.A. (1996b) Receptor-mediated effects of ligand availability influence relative mitogenic potencies of epidermal growth factor and transforming growth factor α. J. Cell. Physiol., 166, 512-522.
    • (1996) J. Cell. Physiol. , vol.166 , pp. 512-522
    • Reddy, C.C.1    Wells, A.2    Laffenburger, D.A.3
  • 54
    • 0025797051 scopus 로고
    • Sequential processing of epidermal growth factor in early and late endosomes of rat liver
    • Renfrew, C.A. and Hubbard, A.L. (1991) Sequential processing of epidermal growth factor in early and late endosomes of rat liver. J. Biol. Chem., 266, 4348-4356.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4348-4356
    • Renfrew, C.A.1    Hubbard, A.L.2
  • 55
    • 0029118223 scopus 로고
    • The cellular response to neuregulins is governed by complex interactions of the ErbB receptor family
    • Riese, D.J., van Raaij, T.M. Plowman, G.D., Andrews, G.C. and Stern, D.F. (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    Andrews, G.C.4    Stern, D.F.5
  • 56
    • 0029829040 scopus 로고    scopus 로고
    • The epidermal growth factor receptor couples transforming growth factor-α, heparin-binding epidermal growth factor-like factor, and amphiregulin to Neu, ErbB-3, and ErbB-4
    • Riese, D.J., Kim, E.D., Elenius, K., Buckley, S., Klagsbrun, M., Plowman, G.D. and Stern, D.F. (1996) The epidermal growth factor receptor couples transforming growth factor-α, heparin-binding epidermal growth factor-like factor, and amphiregulin to Neu, ErbB-3, and ErbB-4. J. Biol. Chem., 271, 20047-20052.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20047-20052
    • Riese, D.J.1    Kim, E.D.2    Elenius, K.3    Buckley, S.4    Klagsbrun, M.5    Plowman, G.D.6    Stern, D.F.7
  • 57
    • 0028955388 scopus 로고
    • Epidermal growth factor-related peptides and their receptors in human malignancies
    • Salomon, D.S., Brandt, R., Ciardiello, F. and Normanno, N. (1995) Epidermal growth factor-related peptides and their receptors in human malignancies. Crit. Rev. Oncol. Hematol., 19, 183-232.
    • (1995) Crit. Rev. Oncol. Hematol. , vol.19 , pp. 183-232
    • Salomon, D.S.1    Brandt, R.2    Ciardiello, F.3    Normanno, N.4
  • 58
    • 0022501030 scopus 로고
    • Transforming growth factor α: More potent angiogenic mediator than epidermal growth factor
    • Schreiber, A.B., Winkler, M.E. and Derynck, R. (1986) Transforming growth factor α: more potent angiogenic mediator than epidermal growth factor. Science, 232, 1250-1253.
    • (1986) Science , vol.232 , pp. 1250-1253
    • Schreiber, A.B.1    Winkler, M.E.2    Derynck, R.3
  • 59
    • 0029011218 scopus 로고
    • The MAP kinase signaling cascade
    • Seger, R. and Krebs, E.G. (1995) The MAP kinase signaling cascade. FASEB J., 9, 726-735.
    • (1995) FASEB J. , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 60
    • 37049183697 scopus 로고
    • Human breast cancer: Correlation of relapse and survival with amplification of the HER-2/neu oncogene
    • Slamon, D.J., Clark, G.M., Wong, S.G., Levin, W.J., Ullrich, A. and McGuire, W.L. (1987) Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science, 235, 177-182.
    • (1987) Science , vol.235 , pp. 177-182
    • Slamon, D.J.1    Clark, G.M.2    Wong, S.G.3    Levin, W.J.4    Ullrich, A.5    McGuire, W.L.6
  • 62
    • 0028302018 scopus 로고
    • ErbB3 is involved in activation of phosphatidylinositol 3-kinase by epidermal growth factor
    • Soltoff, S.P., Carraway, K.L., Prigent, S.A., Gullick, W.G. and Cantley, L.C. (1994) ErbB3 is involved in activation of phosphatidylinositol 3-kinase by epidermal growth factor. Mol. Cell Biol., 14, 3550-3558.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 3550-3558
    • Soltoff, S.P.1    Carraway, K.L.2    Prigent, S.A.3    Gullick, W.G.4    Cantley, L.C.5
  • 63
    • 0027620152 scopus 로고
    • Endocytosis of growth factor receptors
    • Sorkin, A. and Waters, C.M. (1993) Endocytosis of growth factor receptors. BioEssays, 15, 375-382.
    • (1993) BioEssays , vol.15 , pp. 375-382
    • Sorkin, A.1    Waters, C.M.2
  • 64
    • 0027382449 scopus 로고
    • The carboxyl terminus of epidermal growth factor receptor/erbB-2 chimera is internalization impaired
    • Sorkin, A., Di Fiore, P.P. and Carpenter, G. (1993) The carboxyl terminus of epidermal growth factor receptor/erbB-2 chimera is internalization impaired. Oncogene, 8, 3021-3028.
    • (1993) Oncogene , vol.8 , pp. 3021-3028
    • Sorkin, A.1    Di Fiore, P.P.2    Carpenter, G.3
  • 65
    • 0028248951 scopus 로고
    • Molecular and clinical aspects of the Neu/ErbB-2 receptor tyrosine kinase
    • Stancovski, I., Sela, M. and Yarden, Y. (1994) Molecular and clinical aspects of the Neu/ErbB-2 receptor tyrosine kinase. Cancer Treat. Res., 71, 161-191.
    • (1994) Cancer Treat. Res. , vol.71 , pp. 161-191
    • Stancovski, I.1    Sela, M.2    Yarden, Y.3
  • 66
    • 0024673026 scopus 로고
    • Characterization of degP, a gene required for proteolysis in the cell envelope and for growth of Escherichia coli at high temperature
    • Strauch, K.L., Johnson, K. and Beckwith, J. (1989) Characterization of degP, a gene required for proteolysis in the cell envelope and for growth of Escherichia coli at high temperature. J. Bacteriol., 171, 2689-2696.
    • (1989) J. Bacteriol. , vol.171 , pp. 2689-2696
    • Strauch, K.L.1    Johnson, K.2    Beckwith, J.3
  • 67
    • 0032549036 scopus 로고    scopus 로고
    • The ErbB-2/HER2 oncogenic receptor of adenocarcinomas: From orphanhood to multiple stromal ligands
    • Tzahar, E. and Yarden, Y. (1998) The ErbB-2/HER2 oncogenic receptor of adenocarcinomas: from orphanhood to multiple stromal ligands. BBA Rev. Cancer, 1377, M25-M37.
    • (1998) BBA Rev. Cancer , vol.1377
    • Tzahar, E.1    Yarden, Y.2
  • 68
    • 0027971393 scopus 로고
    • ErbB-3 and ErbB-4 function as the respective low and high affinity receptors of all Neu differentiation factor/heregulin isoforms
    • Tzahar, E., Levkowitz, G., Karunagaran, D., Yi, L., Peles, E., Lavi, S., Chang, D., Liu, N., Yayon, A., Wen, D. and Yarden, Y. (1994) ErbB-3 and ErbB-4 function as the respective low and high affinity receptors of all Neu differentiation factor/heregulin isoforms. J. Biol. Chem., 269, 25226-25233.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25226-25233
    • Tzahar, E.1    Levkowitz, G.2    Karunagaran, D.3    Yi, L.4    Peles, E.5    Lavi, S.6    Chang, D.7    Liu, N.8    Yayon, A.9    Wen, D.10    Yarden, Y.11
  • 69
    • 0029814271 scopus 로고    scopus 로고
    • A hierarchical network of inter-receptor interactions determines signal transduction by NDF/neuregulin and EGF
    • Tzahar, E., Waterman, H., Chen, X., Levkowitz, G., Karunagaran, D., Lavi, S., Ratzkin, B.J. and Yarden, Y. (1996) A hierarchical network of inter-receptor interactions determines signal transduction by NDF/neuregulin and EGF. 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
  • 71
    • 0029114837 scopus 로고
    • A single amino acid exchange. Arg-45 to Ala, generates an epidermal growth factor (EGF) mutant with hjgh affinity for the chicken EGF receptor
    • van de Poll, M.L.M., Lenferink, A.E.G., van Vugt, M.J.H., Jacobs, J.J.L., Janssen, J.W.H., Joldersma, M. and van Zoelen, E.J.J. (1995) A single amino acid exchange. Arg-45 to Ala, generates an epidermal growth factor (EGF) mutant with hjgh affinity for the chicken EGF receptor. J. Biol. Chem., 270, 22337-22343.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22337-22343
    • Van De Poll, M.L.M.1    Lenferink, A.E.G.2    Van Vugt, M.J.H.3    Jacobs, J.J.L.4    Janssen, J.W.H.5    Joldersma, M.6    Van Zoelen, E.J.J.7
  • 72
    • 0028170817 scopus 로고
    • Receptor protein-tyrosine kinases and their signal transduction pathways
    • van der Geer, P., Hunter, T. and Lindberg, R.A. (1994) Receptor protein-tyrosine kinases and their signal transduction pathways. Ann. Rev. Cell Biol., 10, 251-337.
    • (1994) Ann. Rev. Cell Biol. , vol.10 , pp. 251-337
    • Van Der Geer, P.1    Hunter, T.2    Lindberg, R.A.3
  • 73
    • 0022967006 scopus 로고
    • Transforming growth factor-β and retinoic aid modulate phenotypic transformation of normal rat kidney cells by epidermal growth factor and platelet-derived growth factor
    • van Zoelen, E.J.J., van Oostwaard, T.M.J. and de Laat, S.W. (1986) Transforming growth factor-β and retinoic aid modulate phenotypic transformation of normal rat kidney cells by epidermal growth factor and platelet-derived growth factor. J. Biol. Chem., 261, 5003-5009.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5003-5009
    • Van Zoelen, E.J.J.1    Van Oostwaard, T.M.J.2    De Laat, S.W.3
  • 75
    • 0025647921 scopus 로고
    • Resistance to receptor-mediated degradation of a murine epidermal growth factor analogue (EGF-Val-47) potentiates its mitogenic activity
    • Walker, F., Nice, E., Fabri, L., Moy, F.J., Liu, J.-F., Wu, R., Scheraga, H.A. and Burgess, A.W. (1990) Resistance to receptor-mediated degradation of a murine epidermal growth factor analogue (EGF-Val-47) potentiates its mitogenic activity. Biochemistry, 29, 10635-10640.
    • (1990) Biochemistry , vol.29 , pp. 10635-10640
    • Walker, F.1    Nice, E.2    Fabri, L.3    Moy, F.J.4    Liu, J.-F.5    Wu, R.6    Scheraga, H.A.7    Burgess, A.W.8
  • 76
    • 0029162564 scopus 로고
    • Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3
    • Wallasch, C. Weiss, F.U., Niederfellner, G., Jallal, B., Issing, W. and Ullrich, A. (1995) Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. EMBO J., 14, 4267-4275.
    • (1995) EMBO J. , vol.14 , pp. 4267-4275
    • Wallasch, C.1    Weiss, F.U.2    Niederfellner, G.3    Jallal, B.4    Issing, W.5    Ullrich, A.6
  • 77
    • 0032577487 scopus 로고    scopus 로고
    • Alternative intracellular routing of ErbB receptors may determine signaling potency
    • Waterman, H., Sabanai, I., Geiger, B. and Yarden, Y. (1998) Alternative intracellular routing of ErbB receptors may determine signaling potency. J. Biol. Chem., 273, 13819-13827.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13819-13827
    • Waterman, H.1    Sabanai, I.2    Geiger, B.3    Yarden, Y.4
  • 78
    • 0024505028 scopus 로고
    • A point mutation in the neu oncogene mimics ligand induction of receptor aggregation
    • Weiner, D.B., Liu, J., Cohen, J.A., Williams, W.V. and Greene, M.I. (1989) A point mutation in the neu oncogene mimics ligand induction of receptor aggregation. Nature, 339, 230-231.
    • (1989) Nature , vol.339 , pp. 230-231
    • Weiner, D.B.1    Liu, J.2    Cohen, J.A.3    Williams, W.V.4    Greene, M.I.5
  • 79
    • 0025139326 scopus 로고
    • Ligand-induced transformation by a non-internalizing epidermal growth factor receptor
    • Wells, A., Welsh, J.B., Lazar, C.S., Wiley, H.S., Gill, G.N. and Rosenfeld, M.G. (1990) Ligand-induced transformation by a non-internalizing epidermal growth factor receptor. Science, 247, 962-964.
    • (1990) Science , vol.247 , pp. 962-964
    • Wells, A.1    Welsh, J.B.2    Lazar, C.S.3    Wiley, H.S.4    Gill, G.N.5    Rosenfeld, M.G.6
  • 80
    • 0030968648 scopus 로고    scopus 로고
    • Structural aspects of the epidermal growth factor receptor required for transmodulation of erbB-2/neu
    • Worthylake, R. and Wiley, H.S. (1997) Structural aspects of the epidermal growth factor receptor required for transmodulation of erbB-2/neu. J. Biol. Chem., 272, 8594-8601.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8594-8601
    • Worthylake, R.1    Wiley, H.S.2
  • 81
    • 0030064531 scopus 로고    scopus 로고
    • Transformation of NIH 3T3 cells by HER3 or HER4 receptors requires the presence of HER1 or HER2
    • Zhang, K., Sun, J., Liu, N., Wen, D., Chang, D., Thomason, A. and Yoshinaga, S.K. (1996) Transformation of NIH 3T3 cells by HER3 or HER4 receptors requires the presence of HER1 or HER2. J. Biol. Chem., 271, 3884-3890.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3884-3890
    • Zhang, K.1    Sun, J.2    Liu, N.3    Wen, D.4    Chang, D.5    Thomason, A.6    Yoshinaga, S.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.