Phosphorylation of the SHC proteins on tyrosine correlates with the transformation of fibroblasts and erythroblasts by the v-sea tyrosine kinase.
Oncogene
; 9(2): 537-44, 1994 Feb.
Article
em En
| MEDLINE
| ID: mdl-8290264
ABSTRACT
The S13 avian erythroblastosis viral genome encodes an oncogenic tyrosine kinase, termed env-sea, that is capable of transforming fibroblasts and erythroblasts. Although the tyrosine kinase activity of the env-sea protein has been shown to be necessary for transformation, no substrates for this enzyme have been detected in vivo. Here we demonstrate that the recently described shc proteins are phosphorylated on tyrosine residues in both S13 transformed fibroblasts and erythroblasts. Furthermore, using an S13 temperature sensitive mutant, we show that the phosphorylation of the shc proteins occurs concomitantly with the activation of the tyrosine kinase activity of the env-sea protein. These observations make the phosphorylation of the shc proteins a good candidate for being involved in oncogenic signaling by the env-sea oncoprotein.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfolipases Tipo C
/
Tirosina
/
Proteínas
/
Proteínas Oncogênicas Virais
/
Eritroblastos
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Fosfotransferases (Aceptor do Grupo Álcool)
/
Proteínas Adaptadoras de Transdução de Sinal
/
Fibroblastos
Limite:
Animals
Idioma:
En
Ano de publicação:
1994
Tipo de documento:
Article