Src-dependent association of Cas and p85 phosphatidylinositol 3'-kinase in v-crk-transformed cells
| Autor: | Rebecca B, Riggins, Regina M, DeBerry, Maziar D, Toosarvandani, Amy H, Bouton |
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| Rok vydání: | 2003 |
| Předmět: |
Retinoblastoma-Like Protein p130
Macromolecular Substances Retroviridae Proteins Oncogenic Proteins Phosphoproteins Transfection Rats Adaptor Proteins Vesicular Transport Phosphatidylinositol 3-Kinases Protein Subunits Cell Transformation Neoplastic Crk-Associated Substrate Protein src-Family Kinases COS Cells Animals Humans Oncogene Protein v-crk Cell Line Transformed Protein Binding |
| Zdroj: | Molecular cancer research : MCR. 1(6) |
| ISSN: | 1541-7786 |
| Popis: | Cellular changes associated with oncogenic transformation are generally caused by deregulation of signal transduction pathways. We show that, in cells transformed by the v-crk oncogene, the adapter protein Cas forms a stable complex with the p85 regulatory subunit of phosphatidylinositol 3'-kinase (PI3K) coincident with the appearance of Cas-associated PI3K activity. The interaction between Cas and p85 PI3K appears to be driven primarily by Src-dependent tyrosine phosphorylation of Cas, and mapping studies indicate that the carboxyl terminus of Cas is necessary and sufficient for binding to p85 PI3K. One of the cellular effects of v-Crk expression is to promote DNA synthesis in the presence of low serum. This effect is potentiated in Cas-null fibroblasts when wild-type Cas is expressed, but not when a Cas variant is expressed that lacks the carboxyl-terminal p85 PI3K binding region. This suggests that the association of Cas with p85 PI3K may play a role in uncoupling growth regulatory pathways through v-Crk. |
| Databáze: | OpenAIRE |
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