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Science 23 February 1990:
Vol. 247. no. 4945, pp. 962 - 964
DOI: 10.1126/science.2305263
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Articles

Science, Vol 247, Issue 4945, 962-964
Copyright © 1990 by American Association for the Advancement of Science

articles

Ligand-induced transformation by a noninternalizing epidermal growth factor receptor

A Wells, JB Welsh, CS Lazar, HS Wiley, GN Gill, and MG Rosenfeld

Department of Pathology, University of California-San Diego, La Jolla 92093.

Identification of a mutant epidermal growth factor (EGF) receptor that does not undergo downregulation has provided a genetic probe to investigate the role of internalization in ligand-induced mitogenesis. Contact-inhibited cells expressing this internalization-defective receptor exhibited a normal mitogenic response at significantly lower ligand concentrations than did cells expressing wild-type receptors. A transformed phenotype and anchorage-independent growth were observed at ligand concentrations that failed to elicit these responses in cells expressing wild-type receptors. These findings imply that activation of the protein tyrosine kinase activity at the cell membrane is sufficient for the growth-enhancing effects of EGF. Thus, downregulation can serve as an attenuation mechanism, without which transformation ensues.


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M. Zhang, M. H. Wang, R. K. Singh, A. Wells, and G. P. Siegal (1997)
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Structural Aspects of the Epidermal Growth Factor Receptor Required for Transmodulation of erbB-2/neu.
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J. Biol. Chem. 270, 24642-24645
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