Desensitization of the EGF receptor alters its ability to undergo EGF-induced dimerization.
Treatment of A431 cells with EGF has been shown to induce the formation of EGF receptor dimers. Sucrose density gradient centrifugation as well as surface radio-iodination followed by crosslinking were used to study further the properties of EGF receptor monomers and dimers as well as the regulation of dimer formation. We have shown previously that treatment of A431 cells with high doses of EGF at 37 degrees C leads to the desensitization of the EGF receptor without a significant loss of cell surface 125I-EGF binding [Kuppuswamy and Pike (1989) J. biol. Chem. 264, 3357-3363; Cunningham et al. (1989) J. biol. Chem. 264, 15351-15356]. Desensitization of the EGF receptor led to a decrease in the ability of receptor monomers to be induced to form dimers by EGF both in vivo and in vitro. These data suggest that the sensitivity of a cell to EGF may be modulated by altering the capacity of the EGF receptor to form oligomers.
Kuppuswamy
D
D
Howard Hughes Medical Institute, Washington University School of Medicine, Department of Biochemistry and Molecular Biophysics, St. Louis, MO 63110.
Pike
L J
LJ
D001667:Binding, Competitive / Q000187:drug effects; D002460:Cell Line; D002478:Cells, Cultured; D003432:Cross-Linking Reagents; D015536:Down-Regulation / Q000187:drug effects*; D004815:Epidermal Growth Factor / Q000494:pharmacology*; D066246:ErbB Receptors / Q000737:chemistry / Q000187:drug effects*; D008968:Molecular Conformation; D015398:Signal Transduction / Q000187:drug effects*
D003432:Cross-Linking Reagents; D004815:Epidermal Growth Factor; D066246:ErbB Receptors