The identification of p130cas-binding proteins and their role in cellular transformation
| Autor: | M R, Burnham, M T, Harte, A, Richardson, J T, Parsons, A H, Bouton |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Retinoblastoma-Like Protein p130
Recombinant Fusion Proteins Proteins Protein-Tyrosine Kinases Proto-Oncogene Proteins c-crk Phosphoproteins src Homology Domains Cellular Apoptosis Susceptibility Protein Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases Proto-Oncogene Proteins Tyrosine Phosphorylation Carrier Proteins Cell Adhesion Molecules Glutathione Transferase |
| Zdroj: | Oncogene. 12(11) |
| ISSN: | 0950-9232 |
| Popis: | Adaptor proteins play an important role in signal transduction by regulating the establishment and maintenance of functionally important protein complexes. A recently described member of this group of proteins is p130cas (CAS), which contains numerous sequence motifs predicted to be involved in mediating protein-protein interactions. We propose that adaptor molecules like CAS may help determine the response of a cell to a particular signal by interacting with specific subsets of cellular proteins. To test this hypothesis, we have identified potential binding partners of CAS that may play a rote in cellular transformation by the oncoproteins v-SRC and/or v-CRK. We show that individual domains of CAS associate with specific subsets of proteins in vitro, and that many of these interactions are dependent on the state of tyrosine-phosphorylation of CAS. Sequences necessary for interacting with the focal adhesion kinase pp125FAK (FAK), v-SRC and v-CRK have been mapped to distinct regions of CAS. In addition, the identification of a number of putative CAS-binding partners that are present in crk-transformed cell extracts but undetectable in normal and src-transformed cell extracts supports a model in which unique protein complexes are formed in response to different signals. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|