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PMID: 2901952 Published · ppublish English Journal Article

Egf binding to its receptor triggers a rapid tyrosine phosphorylation of the erbB-2 protein in the mammary tumor cell line SK-BR-3.

The EMBO journal ·Vol. 7 ·No. 6 ·1988-06-00 ·Pages 1647-51

King CR, Borrello I, Bellot F, Comoglio P, Schlessinger J

Abstract

The epidermal growth factor receptor (EGF-R) and the erbB-2 proto-oncogene product protein are closely related by their structural homology and their shared enzymatic activity as autophosphorylating tyrosine kinases. We show that in mammary tumor cells (SK-BR-3) EGF causes a rapid increase in tyrosine phosphorylation of the erbB-2 protein. Phosphorylation of erbB-2 does not occur in cells lacking the EGF-R (MDA-MB-453). Phosphorylation of erbB-2 in SK-BR-3 cells is blocked if EGF is prevented from interacting with its receptor by specific monoclonal antibodies. While EGF induces the down-regulation of its receptor in SK-BR-3 cells, EGF has no effect on the stability of the erbB-2 protein. This result suggests that the erbB-2 protein is a substrate of the EGF-R and indicates the possibility of communication between these two proteins early in the signal transduction process.

MeSH Terms
Breast Neoplasms/metabolism,pathology Epidermal Growth Factor/metabolism ErbB Receptors/metabolism Humans Phosphorylation Protein Processing, Post-Translational Protein-Tyrosine Kinases/metabolism Proto-Oncogene Mas Proto-Oncogene Proteins/metabolism Receptor, ErbB-2 Tumor Cells, Cultured Tyrosine/metabolism
Chemicals
MAS1 protein, human Proto-Oncogene Mas Proto-Oncogene Proteins Tyrosine Epidermal Growth Factor ErbB Receptors Protein-Tyrosine Kinases Receptor, ErbB-2
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
King C R
Rorer Biotechnology Inc., King of Prussia, PA 19406.
Borrello I
Bellot F
Comoglio P
Schlessinger J
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42 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1988-06-00
Pages
1647-51
Language
English
Region
England
NLM ID
8208664
PMCID
PMC457148
Subset
IM
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