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PMID: 2907606 Published · ppublish English Journal Article

Different structural alterations upregulate in vitro tyrosine kinase activity and transforming potency of the erbB-2 gene.

Molecular and cellular biology ·Vol. 8 ·No. 12 ·1988-12-00 ·Pages 5570-4

Segatto O, King CR, Pierce JH, Di Fiore PP, Aaronson SA

Abstract

Compared with normal erbB-2 gp185, mutant erbB-2 proteins generated by mutations either in the transmembrane domain or by NH2-terminal deletion are able to transform NIH 3T3 cells at a 10- to 100-fold greater efficiency. Mutant proteins of both classes show increased tyrosine kinase activity, suggesting that an abnormal level of receptor-associated tyrosine kinase activity is a major determinant of erbB-2 oncogenic potential.

MeSH Terms
Animals Cell Transformation, Neoplastic Cells, Cultured Genes Genes, Regulator Mice Oncogenes Protein-Tyrosine Kinases/biosynthesis,genetics,metabolism Proto-Oncogene Proteins/biosynthesis,genetics Receptor, ErbB-2
Chemicals
Proto-Oncogene Proteins Protein-Tyrosine Kinases Receptor, ErbB-2
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Segatto O
Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892.
King C R
Pierce J H
Di Fiore P P
Aaronson S A
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.8.12.5570-5574.1988
Published
1988-12-00
Pages
5570-4
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC365664
Subset
IM
External Links
PubMed source DOI: 10.1128/mcb.8.12.5570-5574.1988 PMC Full Text View journal details
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