Abstract
The epidermal growth factor (EGF) receptor is a single chain transmembrane glycoprotein with ligand-dependent protein tyrosine kinase activity (Carpenter, 1987). Activation of the receptor tyrosine kinase is essential, although not necessarily sufficient, for the multiple biological effects of EGF (Chen et al., 1987; Moolenaar et al.,1988). Early events induced by EGF include tyrosine-specific protein phosphorylations, inositol lipid breakdown, changes in cytoplasmic pH and free Ca2+ and alterations in membrane potential (Carpenter, 1987; Chen et al, 1987; Moolenaar et al, 1986 and 1988; Rothenberg et al, 1982; Tilly et al., 1988; Pandiella et al., 1989). This chapter briefly summarizes our recent findings on two aspects of EGF receptor function: ligand-dependent receptor activation with emphasis on the proposed role of ‘receptor dimerization’ and post-receptor signal transduction, particularly the activation of phosphoinositide-specific phospholipase C.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Berridge, M.J. (1987). Ann. Rev. Biochem. 56, 159–193
Boni-Schnetzler, M. & Pilch, P.F. (1987). Proc.Natl.Acad.Sci.USA 84, 7832–78362
Boyer, J.L., Hepler, J.R., and Harden T.K. (1989). Trends Pharmacol. Sci. 10, 360–364
Carpenter, G. (1987). Ann. Rev. Biol. Chem. 56, 881–914
Cassel, D. & Glaser, L (1982). J. Biol. Chem. 257, 9845–9848
Chen, W.S., Lazar, C.S., Poenie, M., Tsien, R.Y., Gill, G.N. & Rosenfeld, M.G. (1987). Nature 328, 820–823
Cochet, C., Gill, G.N., Meisenhelder, J., Cooper, J.A. & Hunter, T. (1984). J.Biol.Chem. 259, 2553–2558
Cochet, C., Kashles, O., Chambaz, E.M., Borrello, I., King, C.R., & Schlessinger, J. (1988). J.Biol.Chem. 26, 33290–3295
Cockcroft, S. (1987). Trends Biochem. Sci. 12, 75–78
Cummings, R.D., Soderquist, A.M. & Carpenter, G. (1985). J.Biol. Chem. 260, 11944–11952
Davis, R.J. (1988). J.Biol.Chem 263, 9462–94694
Fanger, B.D., Stephens, J.E. & Staros, J. (1989). FASEB J. 3, 71–75
Fearn, J.C. & King, A.C. (1985). Cell 40, 991–1000
Friedman, B., van Amsterdam, J, Fusiki, H. & Rosner, M.R. (1989). Proc. Natl. Acad. Sci. USA. 86, 812–816
Friedman, B., Franckelton Jr., A.R., Ross, A.A., Conners, J.M., Fujiki, H., Sugimura, T. & Rosner, M.R. (1984). Proc.Natl.Acad.Sci.USA. 81, 3034–3038
Fuhrmann, U., Bause, E., Legier, G. & Ploegh, H.L. (1984). Nature 307, 755–758
Ghosh-Dastidar, P. & Fox, C.F. (1984). J.Biol.Chem. 259, 3864–3869
Hanley, M.R., and Jackson, T. (1987). Nature 329, 766–767
Hasegawa-Sasaki, H., Lutz, F., and Sasaki, T. (1988). J.Biol. Chem. 263, 12970–12976
Hepler, J.R., Jeffs, R.A., Huckle, W.R., Outlaw, H.E., Rhee, S.G., Earp, H.S., and Harden, T.K. (1990). Biochem. J. 279, 337–344
Honegger, A.M., Dull, T.J., Felder, S., Van Obberghen, E., Bellot, F., Szapary, D., Schmidt, A., Ullrich, A., and Schlessinger, J. (1987). Cell 51, 199–209
Honegger, A.M., Kris, R.M., Ullrich, A. & Schlessinger, J. (1989). Proc. Natl.Acad.Sci. USA. 86, 925–929
Honegger, A.M., Schmidt, A., Ullrich, A., and Schlessinger, J.(1990). Mol. Cell. Biol. 10, 4035–4044
Howell, T.W., and Gomperts, B.D. (1987). Biochim. Biophys. Acta. 927, 177–183
Huang, C. and Ives, H.E. (1989). J. Biol. Chem. 264, 4391–4397
Hunter, T., and Cooper, J.A. (1985). Ann. Rev. Biochem. 54, 897–930
Hunter, T., Ling, N., & Cooper, J.A. (1984). Nature 311, 480–483
Iwashita S., Mitsui, K-i., Shoji-Kasai and Sensu-Miyaike M., (1990). J. Biol. Chem. 265, 10702–10708
Johnson, R.M., and Garrison (1987). J. Biol. Chem. 262, 17285–17293
Jalink K., van Corven, E., and Moolenaar W.H. (1990). J. Biol. Chem. 265, 12232–12239
Kamata, T., and Kung, H.F. (1988). Proc. Natl. Acad. Sci. USA 85, 5799–5803
Kashles, O., Szapary, D., Bellot, F., Ullrich, A., Schlessinger, J. & Schmidt, A. (1988). Proc. Natl.Acad.Sci.USA. 85, 9567–9571
King, C.S. & Cooper, J. (1986). J.Biol.Chem. 261, 10073–10078
Koland, J.G. & Cerione, R.A. (1988). J. Biol. Chem. 263, 2230–2237
Korc, M., Matrisian, L.M. & Magun, B.E. (1984). Proc.Natl.Acad.Sci.USA. 81, 461–465
Lax, I., Bellot, F., Honegger, A.M., Schmidt, A., Ullrich, A., Givol, D., and Schlessinger, J. (1990). Cell Regulation, 1, 173–188
Livneh, E., Dull, T.J., Berent, E., Ullrich, A. & Schlessinger, J. (1988). Mol.Cell.Biol. 8, 48–53
Luttrell, L.M., Hewlett, E.L., Romero, G., and Rogol, A.D. (1988). J. Biol. Chem. 263, 6134–6141
Margolis, B., Rhee, S.G., Felder, S., Mervic, M., Lyall, R., Levitzki, A., Ullrich, A., Zilberstein, A., and Schlessinger, J. (1989). Cell 57, 1101–1107
Martin, T.F.J. (1989). in “Inositol lipids in cell signalling” Michell, R.H., Drummond, A.H., and Downes, C.P. eds. pp 81–112, Acad. Press, New York.
Meisenhelder, J., Suh, P-G., Rhee, S.G., and Hunter, T. (1989). Cell 57, 1109–1122
Moolenaar, W.H., Aerts, R.J., Tertoolen, L.G.J. & de Laat, S.W. (1986). J. Biol. Chem 261, 279–284
Moolenaar, W.H., Bierman, A.J., Tilly, B.C., Verlaan, I., Honegger, A.M., Ullrich, A., and Schlessinger, J. (1988). EMBO 7, 707–710
Nair, B.G., Rashed, H.M. and Patel, T.B. (1989). Biochem. J. 264, 563–571
Nishizuka, Y. (1986). Science 233, 305–312
Northwood, I.C. & Davis, R.J. (1988). J. Biol. Chem. 263, 7450–7453
Northwood, I.C. & Davis, R.J. (1989). J.Biol. Chem. 264, 5746–5750
Pandiella A., Magni, M., Lovisolo, D. and Meldolesi, J. (1989). J. Biol. Chem 264, 12914–12921
Pessin, J.E., Gitomer, W., Oka, Y., Oppenheimer, L. & Czech, M.P. (1983). J. Biol.Chem. 25, 7386–7394
Pike, L.J., and Eakes, A.T. (1987). J. Biol. Chem. 262, 1644–1651
Rothenberg, P., Reuss, L. & Glaser, L. (1982). Proc.Natl.Acad.Sci.USA. 79, 7783–7787
Schlessinger, J. (1988). TIBS 13, 443–447
Slieker, L., Todd, J., Martensen, M. & Lane, M. (1986). J. Biol.Chem. 261, 15233–15241
Smith, C.D., Uhing, R.J., and Snyderman, R. (1987). J. Biol. Chem 262, 6121–6127
Soderquist, A.M. & Carpenter, G. (1984). J.Biol.Chem. 259, 12586–12594
Sturani, E., Zippel, R., Toschi, L., Morello, L., Comoglio, P.M. & Alberghina, L (1988). Mol.Cell.Biol. 8, 1345–1351
Teitelbaum, I. (1990). J. Biol. Chem. 265, 4218–4222
Tilly, B.C., Tertoolen, L.G.J., Lambrechts, A.C., Remorie, R., de Laat, S.W. & Moolenaar, W.H. (1990). Biochem. J. 266, 235–243
Tilly, B.C., van Paridon, P.A., Verlaan, I., de Laat, S.W., and Moolenaar, W.H. (1988). Biochem. J. 252, 857–863
Uhing, R.J., Prpic, V., Jiang, H., and Exton, J.H. (1986). J. Biol. Chem. 261, 2140–2146
van Corven, E.J., Groenink, A., Jalink, K., Eichholtz, T. and Moolenaar, W.H. (1989). Cell 59, 45–54
Verheijden, G. F., Verlaan, I., van lersel, M., and Moolenaar, W.H. (1990). Biochem. J. 271, 215–221
Verheijden, G.F., Verlaan, I., and Moolenaar, W.M. (1990). Cell Regulation 1, 615–620
Wahl, M.I., and Carpenter, G. (1988). J. Biol. Chem. 263, 7581–7590
Wahl, M.I., Nishibe, S., Kim, J.W., Kim, H., Rhee, S.G. and Carpenter, G. (1990). J. Biol. Chem. 265, 3944–3948
Whiteley, B. & Glaser, L (1986). J.Cell. Biol. 103, 1355–1362
Yarden, Y. & Schlessinger J. (1987). Biochemistry 26, 1434–1442
Yarden, Y. & Schlessinger J. (1987). Biochemistry 26, 1443–1451
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1991 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Verheijden, G.F., Verlaan, I., Moolenaar, W.H. (1991). The Epidermal Growth Factor Receptor: Receptor Dimerization and Signal Transduction. In: Ross, E.M., Wirtz, K.W.A. (eds) Biological Signal Transduction. NATO ASI Series, vol 52. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75136-3_3
Download citation
DOI: https://doi.org/10.1007/978-3-642-75136-3_3
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-75138-7
Online ISBN: 978-3-642-75136-3
eBook Packages: Springer Book Archive