메뉴 건너뛰기




Volumn 16, Issue 1, 1998, Pages 53-67

Biochemical characterization of mutant EGF receptors expressed in the hemopoietic cell line BaF/3

Author keywords

Affinity; Epidermal growth factor receptor; Phosphorylation; Structure; Tyrosine kinase

Indexed keywords

ADENOSINE TRIPHOSPHATE; EPIDERMAL GROWTH FACTOR RECEPTOR; MUTANT PROTEIN; PHOSPHOTRANSFERASE; PROTEIN TYROSINE KINASE;

EID: 0031795791     PISSN: 08977194     EISSN: None     Source Type: Journal    
DOI: 10.3109/08977199809017491     Document Type: Article
Times cited : (30)

References (43)
  • 1
    • 0025020407 scopus 로고
    • High-affinity epidermal growth factor binding is specifically reduced by a monoclonal antibody, and appears necessary for early responses
    • Bellot, F., Molenaar, W., Kris, K., Mirakhur, B., Verlaan, I., Ullrich, A., Schlessinger, J. and Felder, S. (1990) High-affinity epidermal growth factor binding is specifically reduced by a monoclonal antibody, and appears necessary for early responses. J. Cell Biol. 110, 491-502.
    • (1990) J. Cell Biol. , vol.110 , pp. 491-502
    • Bellot, F.1    Molenaar, W.2    Kris, K.3    Mirakhur, B.4    Verlaan, I.5    Ullrich, A.6    Schlessinger, J.7    Felder, S.8
  • 2
    • 0021008434 scopus 로고
    • Murine epidermal growth factor: Heterogeneity on high resolution ion-exchange chromatography
    • Burgess, A.W., Lloyd, C.J. and Nice, E.C. (1983) Murine epidermal growth factor: heterogeneity on high resolution ion-exchange chromatography. EMBO J. 2, 2065-2069.
    • (1983) EMBO J. , vol.2 , pp. 2065-2069
    • Burgess, A.W.1    Lloyd, C.J.2    Nice, E.C.3
  • 3
    • 0028176477 scopus 로고
    • A neu acquaintance for erbB3 and erbB4: A role for receptor heterodimerization in growth signaling
    • Carraway, K.L. III 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. III1    Cantley, L.C.2
  • 4
    • 0026344988 scopus 로고
    • Ligandinduced internalization and increased cell calcium are mediated via distinct structural elements in the carboxyl terminus of the epidermal growth factor receptor
    • Chang, C.P., Kao, J.P., Lazar, C.S., Walsh, B.J., Wells, A., Wiley, H.S., Gill, G.N. and Rosenfeld, M.G. (1991) Ligandinduced internalization and increased cell calcium are mediated via distinct structural elements in the carboxyl terminus of the epidermal growth factor receptor. J. Biol. Chem. 266, 23467-23470.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23467-23470
    • Chang, C.P.1    Kao, J.P.2    Lazar, C.S.3    Walsh, B.J.4    Wells, A.5    Wiley, H.S.6    Gill, G.N.7    Rosenfeld, M.G.8
  • 5
    • 0023238874 scopus 로고
    • Requirement for intrinsic protein tyrosine kinase in the immediate and late actions of the EGF receptor
    • Chen, W.S., Lazar, C.S., Poenie, M., Tsien, R.Y., Gill, G.N. and Rosenfeld, M.G. (1987) Requirement for intrinsic protein tyrosine kinase in the immediate and late actions of the EGF receptor. Nature 328, 820-823.
    • (1987) Nature , vol.328 , pp. 820-823
    • Chen, W.S.1    Lazar, C.S.2    Poenie, M.3    Tsien, R.Y.4    Gill, G.N.5    Rosenfeld, M.G.6
  • 6
    • 0028237038 scopus 로고
    • A kinasenegative epidermal growth factor receptor that retains the capacity to stimulate DNA synthesis
    • Coker, K.J., Staros, J.V. and Guyer, C.A. (1994) A kinasenegative epidermal growth factor receptor that retains the capacity to stimulate DNA synthesis. Proc. Nail. Acad. Sci. USA 91(15), 6967-6971.
    • (1994) Proc. Nail. Acad. Sci. USA , vol.91 , Issue.15 , pp. 6967-6971
    • Coker, K.J.1    Staros, J.V.2    Guyer, C.A.3
  • 7
    • 0021752924 scopus 로고
    • Human transforming growth factoralpha: Precursor structure and expression in E. coli
    • Derynck, R., Roberts, A.B., Winkler, M.E., Chen, E.Y. and Goeddel, D.V. (1984) Human transforming growth factoralpha: precursor structure and expression in E. coli. Cell 38, 287-297.
    • (1984) Cell , vol.38 , pp. 287-297
    • Derynck, R.1    Roberts, A.B.2    Winkler, M.E.3    Chen, E.Y.4    Goeddel, D.V.5
  • 8
    • 0026574126 scopus 로고
    • Kinetics of binding, endocytosis, and recycling of EGF receptor mutant
    • Felder, S., La Vin, J., Ullrich, A. and Schlessinger, J. (1992) Kinetics of binding, endocytosis, and recycling of EGF receptor mutant. J. Cell. Biol. 117, 203-212.
    • (1992) J. Cell. Biol. , vol.117 , pp. 203-212
    • Felder, S.1    La Vin, J.2    Ullrich, A.3    Schlessinger, J.4
  • 10
    • 0017874586 scopus 로고
    • Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril
    • Fracker, P.J. and Speck, J.C. (1978) Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril. Biochem. Biophys. Commun. 80, 849-857.
    • (1978) Biochem. Biophys. Commun. , vol.80 , pp. 849-857
    • Fracker, P.J.1    Speck, J.C.2
  • 11
    • 0021254542 scopus 로고
    • Monoclonal anti-epidermal growth factor receptor antibodies which are inhibitors of epidermal growth factor binding and antagonists of epidermal growth factor binding and antagonists of epidermal growth factor-stimulated tyrosine protein kinase activity
    • Gill, G.N., Kawamoto, T., Cochet, C., Le, A., Sato, J.D., Masui, H., McLeod, A., and Mendelsohn, J. (1984) Monoclonal anti-epidermal growth factor receptor antibodies which are inhibitors of epidermal growth factor binding and antagonists of epidermal growth factor binding and antagonists of epidermal growth factor-stimulated tyrosine protein kinase activity. J. Biol. Chem. 259, 7755-7760.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7755-7760
    • Gill, G.N.1    Kawamoto, T.2    Cochet, C.3    Le, A.4    Sato, J.D.5    Masui, H.6    McLeod, A.7    Mendelsohn, J.8
  • 12
    • 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.Jr., 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., Jr.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
  • 13
    • 0028049245 scopus 로고
    • Epidermal growth factor-receptor mutant lacking the autophosphorylation sites induces phosphorylation of She protein and Shc-Grb2/ASH association and retains mitogenic activity
    • Gotoh, N., Tojo, A., Muroya, K., Hashimoto, Y., Hattori, S., Nakamura, S., Takenawa, T., Yazaki, Y. and Shibuya, M. (1994) Epidermal growth factor-receptor mutant lacking the autophosphorylation sites induces phosphorylation of She protein and Shc-Grb2/ASH association and retains mitogenic activity. Proc. Natl. Acad. Sci. USA 91, 167-171.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 167-171
    • Gotoh, N.1    Tojo, A.2    Muroya, K.3    Hashimoto, Y.4    Hattori, S.5    Nakamura, S.6    Takenawa, T.7    Yazaki, Y.8    Shibuya, M.9
  • 14
    • 0023820347 scopus 로고
    • The pp60v-src tyrosine kinase desensitizes epidermal growth factor binding to 3T3 fibroblasts by two distinct protein kinase C-independent mechanisms
    • Gray, G.M., and Macara, I.G. (1988) The pp60v-src tyrosine kinase desensitizes epidermal growth factor binding to 3T3 fibroblasts by two distinct protein kinase C-independent mechanisms. J. Biol. Chem. 263, 10714-10719.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10714-10719
    • Gray, G.M.1    Macara, I.G.2
  • 15
    • 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. and Treutlein, H.R. (1997) A model for the activation of the epidermal growth factor receptor kinase involvement of an asymmetric dimer? Biochemistry 36 3826-3836.
    • (1997) Biochemistry , vol.36 , pp. 3826-3836
    • Groenen, L.C.1    Walker, F.2    Burgess, A.W.3    Treutlein, H.R.4
  • 16
    • 0027369657 scopus 로고
    • Expression of human tyrosine kinase-negative epidermal growth factor receptor amplifies signaling through endogenous murine epidermal growth factor receptor
    • Hack, N., Sue-A-Quan, A., Mills, G.B. and Skorecki, K.L. (1993) Expression of human tyrosine kinase-negative epidermal growth factor receptor amplifies signaling through endogenous murine epidermal growth factor receptor. J. Biol. Chem. 268, 26441-26446.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26441-26446
    • Hack, N.1    Sue-A-Quan, A.2    Mills, G.B.3    Skorecki, K.L.4
  • 17
    • 0018849228 scopus 로고
    • Dansylcadaverine inhibits internalization of 1251-epidermal growth factor in BALE 3T3 cells
    • Haigler, H.T., Maxfield, F.R., Willingham, M.C. and Pastan, I. (1980) Dansylcadaverine inhibits internalization of 1251-epidermal growth factor in BALE 3T3 cells. J. Biol. Chem., 257, 1239-1241.
    • (1980) J. Biol. Chem. , vol.257 , pp. 1239-1241
    • Haigler, H.T.1    Maxfield, F.R.2    Willingham, M.C.3    Pastan, I.4
  • 18
    • 0024836051 scopus 로고
    • A restricted cytoplasmic region of IL-2 receptor beta chain is essential for growth signal transduction but not for ligand binding and internalization
    • Hatakeyama, M., Mori, H., Doi, T. and Taniguchi, T. (1989) A restricted cytoplasmic region of IL-2 receptor beta chain is essential for growth signal transduction but not for ligand binding and internalization. Cell 59, 837-845.
    • (1989) Cell , vol.59 , pp. 837-845
    • Hatakeyama, M.1    Mori, H.2    Doi, T.3    Taniguchi, T.4
  • 20
    • 0023663092 scopus 로고
    • Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing
    • Honegger, A.M., Dull, T.J., Felder, S., Van Obberghen, E., Bellot, F., Szapary, D., Schmidt, A., Ullrich, A. and Schlessinger, J. (1987a) Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing. Cell 51, 199-209.
    • (1987) Cell , vol.51 , pp. 199-209
    • Honegger, A.M.1    Dull, T.J.2    Felder, S.3    Van Obberghen, E.4    Bellot, F.5    Szapary, D.6    Schmidt, A.7    Ullrich, A.8    Schlessinger, J.9
  • 21
    • 0023461796 scopus 로고
    • A mutant epidermal growth factor receptor with defective protein tyrosine kinase is unable to stimulate protooncogene expression and DNA synthesis
    • Honegger, A.M., Szapary, D., Scmidt, A., Lyall, R., Van Obberghen, E., Dull, T.J., Ullrich, A. and Schlessinger, J. (1987b) A mutant epidermal growth factor receptor with defective protein tyrosine kinase is unable to stimulate protooncogene expression and DNA synthesis. Mol. Cell. Biol. 7, 4568-4571.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 4568-4571
    • Honegger, A.M.1    Szapary, D.2    Scmidt, A.3    Lyall, R.4    Van Obberghen, E.5    Dull, T.J.6    Ullrich, A.7    Schlessinger, J.8
  • 22
    • 0022654122 scopus 로고
    • Neither arginine nor histidine can carry out the function of lysine-295 in the ATP-binding site of p60src
    • Kamps, M.P. and Sefton, B.M. (1986) Neither arginine nor histidine can carry out the function of lysine-295 in the ATP-binding site of p60src. Mol. Cell. Biol. 6, 751-757.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 751-757
    • Kamps, M.P.1    Sefton, B.M.2
  • 23
    • 0029807139 scopus 로고    scopus 로고
    • Lysosomal targeting of epidermal growth factor receptors via a kinase-dependent pathway is mediated by the receptor carboxyl-terminal residues 1022-1123
    • Kornilova, E., Sorkina, T., Beguinot, L. and Sorkin, A. (1996) Lysosomal targeting of epidermal growth factor receptors via a kinase-dependent pathway is mediated by the receptor carboxyl-terminal residues 1022-1123. J. Biol. Chem. 271(48), 30340-30346.
    • (1996) J. Biol. Chem. , vol.271 , Issue.48 , pp. 30340-30346
    • Kornilova, E.1    Sorkina, T.2    Beguinot, L.3    Sorkin, A.4
  • 24
    • 0024326947 scopus 로고
    • Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: Evidence for overexpression in a subset of human mammary tumors
    • Kraus, M.H., Issing, W., Miki, T., Popescu, N.C. and Aaronson, S.A. (1989) Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: evidence for overexpression in a subset of human mammary tumors. Proc. Natl. Acad. Sci., USA 86, 9193-9197.
    • (1989) Proc. Natl. Acad. Sci., USA , vol.86 , pp. 9193-9197
    • Kraus, M.H.1    Issing, W.2    Miki, T.3    Popescu, N.C.4    Aaronson, S.A.5
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0028950805 scopus 로고
    • Recruitment of epidermal growth factor receptors into coated pits requires their activated tyrosine kinase
    • Lamaze, C. and Schmid, S.L. (1995) Recruitment of epidermal growth factor receptors into coated pits requires their activated tyrosine kinase. J. Cell. Biol. 129, 47-54.
    • (1995) J. Cell. Biol. , vol.129 , pp. 47-54
    • Lamaze, C.1    Schmid, S.L.2
  • 27
    • 0028104202 scopus 로고
    • Regulation of signal transduction and signal diversity by receptor oligomerization
    • Lemmon, M.A. and Schlessinger, J. (1994) Regulation of signal transduction and signal diversity by receptor oligomerization. TIBS 19, 459-463.
    • (1994) TIBS , vol.19 , pp. 459-463
    • Lemmon, M.A.1    Schlessinger, J.2
  • 29
    • 0025655658 scopus 로고
    • Molecular and cellular biology of interleukin-3
    • Morris, C.F., Young, I.G. and Hapel, A.J. (1990) Molecular and cellular biology of interleukin-3. Immunol. Ser. 49, 177-214.
    • (1990) Immunol. Ser. , vol.49 , pp. 177-214
    • Morris, C.F.1    Young, I.G.2    Hapel, A.J.3
  • 31
    • 0022274007 scopus 로고
    • Il-3-dependent mouse clones that express B-220 surface antigen, contain Ig genes in germ-line configuration, and generate B lymphocytes in vivo
    • Palacios, R. and Steinmetz, M. (1985) Il-3-dependent mouse clones that express B-220 surface antigen, contain Ig genes in germ-line configuration, and generate B lymphocytes in vivo. Cell 41, 727-734.
    • (1985) Cell , vol.41 , pp. 727-734
    • Palacios, R.1    Steinmetz, M.2
  • 32
    • 0029928988 scopus 로고    scopus 로고
    • Mutation of position 52 in ERK2 creates a nonproductive binding mode for adenosine 5′-triphosphate
    • Robinson, M.J., Harkins, P.C., Zhang, J., Baer, R., Haycock, J.W., Cobb, M.H. and Goldsmith, F.J. (1996) Mutation of position 52 in ERK2 creates a nonproductive binding mode for adenosine 5′-triphosphate. Biochemistry 35, 5641-5646.
    • (1996) Biochemistry , vol.35 , pp. 5641-5646
    • Robinson, M.J.1    Harkins, P.C.2    Zhang, J.3    Baer, R.4    Haycock, J.W.5    Cobb, M.H.6    Goldsmith, F.J.7
  • 33
    • 0015502174 scopus 로고
    • The primary structure of epidermal growth factor
    • Savage, C.R., Inagami, T. and Cohen, S. (1972) The primary structure of epidermal growth factor. J. Biol. Chem. 247, 7612-7621.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7612-7621
    • Savage, C.R.1    Inagami, T.2    Cohen, S.3
  • 34
    • 0027395165 scopus 로고
    • Mitogen-activated protein kinase stimulation by a tyrosine kinase-negative epidermal growth factor receptor
    • Selva, E., Raden, D.L. and Davis, R.J. (1993) Mitogen-activated protein kinase stimulation by a tyrosine kinase-negative epidermal growth factor receptor. J. Biol. Chem. 268, 2250-2254.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2250-2254
    • Selva, E.1    Raden, D.L.2    Davis, R.J.3
  • 35
    • 0028237504 scopus 로고
    • Potent SHC tyrosine phosphorylation by epidermal growth factor at low receptor density or in the absence of receptor autophosphorylation sites
    • Soler, C., Alvarez, C.V., Beguinot, L. and Carpenter, G. (1994) Potent SHC tyrosine phosphorylation by epidermal growth factor at low receptor density or in the absence of receptor autophosphorylation sites. Oncogene 9, 2207-2215.
    • (1994) Oncogene , vol.9 , pp. 2207-2215
    • Soler, C.1    Alvarez, C.V.2    Beguinot, L.3    Carpenter, G.4
  • 37
    • 0029889579 scopus 로고    scopus 로고
    • Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr974-containing internalization motif
    • Sorkin, A., Mazzotti, M., Sorkina, T., Scotto, L. and Beguinot, L. (1996) Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr974-containing internalization motif. J. Biol. Chem. 271(23), 13377-13384.
    • (1996) J. Biol. Chem. , vol.271 , Issue.23 , pp. 13377-13384
    • Sorkin, A.1    Mazzotti, M.2    Sorkina, T.3    Scotto, L.4    Beguinot, L.5
  • 38
    • 0022588291 scopus 로고
    • P185, a product of the neu proto-oncogene, is a receptor like protein associated with tyrosine kinase activity
    • Stern, D.F., Heffernan, P.A. and Weinberg, R.A. (1986) p185, a product of the neu proto-oncogene, is a receptor like protein associated with tyrosine kinase activity. Mol. Cell. Biol. 6, 1729-1740.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1729-1740
    • Stern, D.F.1    Heffernan, P.A.2    Weinberg, R.A.3
  • 39
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A. and Schlessinger, J. (1990) Signal transduction by receptors with tyrosine kinase activity. Cell 61, 203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 40
    • 0023770018 scopus 로고
    • Transmodulation of the epidermal-growth-factor receptor in permeabilized 3T3 cells
    • Walker, F. and Burgess, A.W. (1988) Transmodulation of the epidermal-growth-factor receptor in permeabilized 3T3 cells. Biochem. J. 256, 109-115.
    • (1988) Biochem. J. , vol.256 , pp. 109-115
    • Walker, F.1    Burgess, A.W.2
  • 41
    • 0027337969 scopus 로고
    • Translocation of pp60c-src from the plasma membrane to the cytosol after stimulation by platelet-derived growth factor
    • Walker, F., deBlaquiere, J. and Burgess, A.W. (1993) Translocation of pp60c-src from the plasma membrane to the cytosol after stimulation by platelet-derived growth factor. J. Biol. Chem. 268, 19552-19558.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19552-19558
    • Walker, F.1    DeBlaquiere, J.2    Burgess, A.W.3
  • 42
    • 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.G., 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.G.2    Fabri, L.3    Moy, F.J.4    Liu, J.F.5    Wu, R.6    Scheraga, H.A.7    Burgess, A.W.8
  • 43
    • 0029067672 scopus 로고
    • An incomplete program of cellular tyrosine phosphorylations induced by kinase-defective epidermal growth factor receptors
    • Wright, J.D., Reuter, C.W. and Weber, M.J. (1995) An incomplete program of cellular tyrosine phosphorylations induced by kinase-defective epidermal growth factor receptors. J. Biol. Chem. 270, 2085-12093.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2085-12093
    • Wright, J.D.1    Reuter, C.W.2    Weber, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.