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.
|Number of pages||6|
|Publication status||Published - 06 Jun 1996|
- Carrier Proteins
- Cell Adhesion Molecules
- Cellular Apoptosis Susceptibility Protein
- Focal Adhesion Kinase 1
- Focal Adhesion Protein-Tyrosine Kinases
- Glutathione Transferase
- Protein-Tyrosine Kinases
- Proto-Oncogene Proteins
- Proto-Oncogene Proteins c-crk
- Recombinant Fusion Proteins
- Retinoblastoma-Like Protein p130
- src Homology Domains
Burnham, M. R., Harte, M. T., Richardson, A., Parsons, J. T., & Bouton, A. H. (1996). The identification of p130cas-binding proteins and their role in cellular transformation. Oncogene, 12(11), 2467-72.