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The related adhesion focal tyrosine kinase is tyrosine-phosphorylated after beta1-integrin stimulation in B cells and binds to p130cas.

http://www.ncbi.nlm.nih.gov/pubmed/8995252

Integrin ligation initiates intracellular signaling events, among which are the activation of protein tyrosine kinases. The related adhesion focal tyrosine kinase (RAFTK), also known as PYK2 and CAKbeta, is a tyrosine kinase that is homologous to the focal adhesion kinase (FAK) p125FAK. The structure of RAFTK is similar to p125FAK in that it lacks a transmembrane region, does not contain Src homology 2 or 3 domains, and has a proline-rich region in its C terminus. Here we report that RAFTK is a target for beta1-integrin-mediated tyrosine phosphorylation in both transformed and normal human B cells. Ligation of the B cell antigen receptor also induced tyrosine phosphorylation of RAFTK. Phosphorylation of RAFTK following integrin- or B cell antigen receptor-mediated stimulation was decreased by prior treatment of cells with cytochalasin B, indicating that this process was at least partially cytoskeleton-dependent. One of the tyrosine-phosphorylated substrates after integrin stimulation in fibroblasts is p130cas, which can associate with p125FAK. RAFTK also interacted constitutively with p130cas in B cells, since p130cas was detected in RAFTK immunoprecipitates. Although the function of RAFTK remains unknown, these data suggest that RAFTK may have a significant function in integrin-mediated signaling pathways in B cells.

Pubmed ID: 8995252 RIS Download

Mesh terms: Antigens, CD29 | B-Lymphocytes | Crk-Associated Substrate Protein | Cytochalasin B | Cytoskeleton | Focal Adhesion Kinase 2 | Humans | Lymphocyte Activation | Macromolecular Substances | Palatine Tonsil | Phosphoproteins | Phosphotyrosine | Protein Binding | Protein-Tyrosine Kinases | Proteins | Receptors, Antigen, B-Cell | Retinoblastoma-Like Protein p130 | Signal Transduction