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PMID: 2464744 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Oncogenic activation of p185neu stimulates tyrosine phosphorylation in vivo.

Molecular and cellular biology ·Vol. 8 ·No. 9 ·1988-09-00 ·Pages 3969-73

Stern DF, Kamps MP, Cao H

Abstract

p185, the product of the neu/erbB2 proto-oncogene, is oncogenically activated by a point mutation that substitutes glutamic acid for valine in the transmembrane domain of the protein. We have found that the transforming form of p185 differs from its normal counterpart in inducing increased tyrosine phosphorylation of other proteins in vivo and in having a much shorter half-life. These results support the model that the transforming p185 resembles a ligand-activated receptor.

MeSH Terms
Animals Cell Line Cell Transformation, Neoplastic Cells, Cultured Gene Expression Regulation Mutation Phosphorylation Phosphotyrosine Protein-Tyrosine Kinases/genetics Proto-Oncogene Proteins/genetics Proto-Oncogenes Receptor, ErbB-2 Transfection Tyrosine/analogs & derivatives,analysis
Chemicals
Proto-Oncogene Proteins Phosphotyrosine Tyrosine Protein-Tyrosine Kinases Receptor, ErbB-2
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Stern D F
Department of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510.
Kamps M P
Cao H
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48 references, click to expand
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.8.9.3969-3973.1988
Published
1988-09-00
Pages
3969-73
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC365461
Subset
IM
Grants
NCI NIH HHS · CA17289 · United States
NCI NIH HHS · CA45708 · United States
External Links
PubMed source DOI: 10.1128/mcb.8.9.3969-3973.1988 PMC Full Text View journal details
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