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J. Biol. Chem., Vol. 265, Issue 3, 1750-1754, Jan, 1990
GM Walton, WS Chen, MG Rosenfeld and GN Gill
The human epidermal growth factor receptor (EGFR) contains a large C'
terminus distal to the protein tyrosine kinase domain that is conserved
among members of its extended gene family. To investigate the C' terminus,
a series of mutant EGFR cDNAs encoding progressive C'- terminal deletions
were prepared and expressed in null recipient B82L cells. In vivo
self-phosphorylation was retained in receptors truncated to residues 1052
and 1022 which lack the three identified sites of tyrosine
self-phosphorylation. Receptors truncated to residue 991 did not undergo in
vivo self-phosphorylation. Purified 1022 truncated receptor was
self-phosphorylated to the extent of 1 mol of phosphate/mol of receptor
protein. The deduced additional site of tyrosine self-phosphorylation at
residue 992 was confirmed by tryptic phosphopeptide mapping and protein
sequencing. EGFRs deleted to give C'- terminal residues 1052, 1022, 991,
and 973 exhibited enhanced EGF- stimulated tyrosine phosphorylation of cell
substrates in vivo, whereas deletion at residue 944 abolished all
detectable EGF-stimulated protein tyrosine phosphorylation. These results
indicate that ligand-induced self-phosphorylation is limited to the C'
terminus of the EGFR and suggest that this region of the holoreceptor has
an inhibitory function.
Analysis of deletions of the carboxyl terminus of the epidermal growth factor receptor reveals self-phosphorylation at tyrosine 992 and enhanced in vivo tyrosine phosphorylation of cell substrates
Department of Medicine, Howard Hughes Medical Institute, University of California, San Diego, School of Medicine, La Jolla 92093.
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