Tyrosine phosphorylation of BCR by FPS/FES protein-tyrosine kinases induces association of BCR with GRB-2/SOS.

The human bcr gene encodes a protein with serine/threonine kinase activity, CDC24/dbl homology, a GAP domain, and an SH2-binding region. However, the precise physiological functions of BCR are unknown. Coexpression of BCR with the cytoplasmic protein-tyrosine kinase encoded by the c-fes proto-oncogene in Sf-9 cells resulted in stable BCR-FES protein ...
complex formation and tyrosine phosphorylation of BCR. Association involves the SH2 domain of FES and a novel binding domain localized to the first 347 amino acids of the FES N-terminal region. Deletion of the homologous N-terminal BCR-binding domain from v-fps, a fes-related transforming oncogene, abolished transforming activity and tyrosine phosphorylation of BCR in vivo. Tyrosine phosphorylation of BCR in v-fps-transformed cells induced its association with GRB-2/SOS, the RAS guanine nucleotide exchange factor complex. These data provide evidence that BCR couples the cytoplasmic protein-tyrosine kinase and RAS signaling pathways.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Animals, Cell Line, Cell Transformation, Neoplastic, Fusion Proteins, gag-onc, GRB2 Adaptor Protein, Guanine Nucleotide Exchange Factors, Humans, Oncogene Proteins, Oncogenes, Phosphorylation, Phosphotyrosine, Protein Binding, Protein-Tyrosine Kinases, Proteins, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-bcr, Receptor, Epidermal Growth Factor, Recombinant Fusion Proteins, Recombinant Proteins, Restriction Mapping, Sequence Deletion, Spodoptera, Transfection, Tyrosine, ras Guanine Nucleotide Exchange Factors
Mol. Cell. Biol.
Date: Feb. 01, 1995
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