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EGF‐stimulated tyrosine phosphorylation of p185neu: a potential model for receptor interactions.
Author(s) -
Stern D. F.,
Kamps M. P.
Publication year - 1988
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1988.tb02906.x
Subject(s) - epidermal growth factor , phosphorylation , stern , tyrosine phosphorylation , receptor tyrosine kinase , biology , haven , receptor , tyrosine , tyrosine kinase , microbiology and biotechnology , biochemistry , history , ancient history , mathematics , combinatorics
p185neu is a receptor‐like protein encoded by the neu/erbB‐2 proto‐oncogene. This protein is closely related to the epidermal growth factor (EGF) receptor, but does not bind EGF. We report here that incubation of Rat‐1 cells with EGF stimulates tyrosine phosphorylation of p185. This effect is specific to EGF since neither platelet derived growth factor (PDGF) nor insulin, which also bind to receptors with ligand‐stimulated tyrosine kinase activity, induced tyrosine phosphorylation of p185. The EGF‐stimulated tyrosine phosphorylation of p185 and of the EGF receptor occurred with similar kinetics and EGF dose‐responses, and both phosphorylations were prevented by down‐regulation of the EGF receptor with EGF. Since p185 does not bind EGF, these results suggested that p185 is a substrate for the EGF receptor kinase. Incubation of cells with EGF before lysis stimulated the tyrosine phosphorylation of p185 in immune complexes. This suggested that EGF, acting through the EGF receptor, can regulate the intrinsic kinase activity of p185.