title: Different structural alterations upregulate in vitro tyrosine kinase activity and transforming potency of the erbB-2 gene.
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.
authors.affiliation: Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892.
authors.forename: O
authors.initials: O
authors.lastname: Segatto
authors.forename: C R
authors.initials: CR
authors.lastname: King
authors.forename: J H
authors.initials: JH
authors.lastname: Pierce
authors.forename: P P
authors.initials: PP
authors.lastname: Di Fiore
authors.forename: S A
authors.initials: SA
authors.lastname: Aaronson
mesh_terms: D000818:Animals; D002471:Cell Transformation, Neoplastic; D002478:Cells, Cultured; D005796:Genes; D005809:Genes, Regulator; D051379:Mice; D009857:Oncogenes; D011505:Protein-Tyrosine Kinases / Q000096:biosynthesis / Q000235:genetics* / Q000378:metabolism; D011518:Proto-Oncogene Proteins / Q000096:biosynthesis / Q000235:genetics*; D018719:Erb-b2 Receptor Tyrosine Kinases
chemical_list: D011505:Protein-Tyrosine Kinases; D011518:Proto-Oncogene Proteins; D018719:Erb-b2 Receptor Tyrosine Kinases