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J. Biol. Chem., Vol. 268, Issue 13, 9176-9179, 05, 1993
SJ Decker
Mutant epidermal growth factor (EGF) receptors in which the five known
tyrosine autophosphorylation sites (tyrosines 992, 1068, 1086, 1148, and
1173) were replaced with phenylalanine residues were expressed in NIH-3T3
cells (5F-EGFR) and transmembrane signaling parameters compared with cells
expressing wild-type EGF receptor (WT-EGFR). Mutant and wild- type clones
were chosen expressing similar numbers of receptors and Scatchard analysis
of 125I-EGF binding showed high and low affinity binding of equal
affinities for both receptor types. EGF stimulated tyrosine phosphorylation
of proteins to a much lesser degree in cells expressing 5F-EGFR relative to
cells expressing WT-EGFR. Tyrosine phosphorylation of the 5F-EGFR was 2-4%
of WT-EGFR. Surprisingly, cells expressing WT-EGFR or 5F-EGFR showed little
difference in dose response of EGF-stimulated [3H]thymidine incorporation
or EGF stimulation of mitogen-activated protein kinase activity. However,
EGF did not induce anchorage-independent growth of cells expressing 5F-EGFR
to the same extent as it did for cells expressing WT-EGFR. EGF treatment of
5F-EGFR cells failed to elicit an increase in phosphatidylinositol 3-kinase
activity or to stimulate hydrolysis of phosphoinositides or tyrosine
phosphorylation of phospholipase C-gamma 1. These data suggest that a
significant proportion of EGF receptor signaling can occur through
receptors with altered capacity to interact with src homology 2 domain-
containing proteins.
Transmembrane signaling by epidermal growth factor receptors lacking autophosphorylation sites
Parke-Davis Pharmaceuticals, Ann Arbor, Michigan 48106.
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