| First Author | Fournel M | Year | 1996 |
| Journal | J Exp Med | Volume | 183 |
| Issue | 1 | Pages | 301-6 |
| PubMed ID | 8551236 | Mgi Jnum | J:35635 |
| Mgi Id | MGI:83082 | Doi | 10.1084/jem.183.1.301 |
| Citation | Fournel M, et al. (1996) Association of tyrosine protein kinase Zap-70 with the protooncogene product p120c-cbl in T lymphocytes. J Exp Med 183(1):301-6 |
| abstractText | Accumulating data show that the tyrosine protein kinase Zap-70 plays an essential role in T cell receptor-mediated signal transduction. However, the model of action, as well as the physiologically relevant substrates of Zap-70, have not been determined. We have attempted to identify a 120-kD tyrosine-phosphorylated protein (p120) that associates with Zap-70 in activated T lymphocytes. The results of our analyses showed that p120 is largely encoded by the c-cbl protooncogene. Furthermore, the association of Zap-70 with c-Cbl was shown to be induced by T cell receptor stimulation, implying that it required posttranslational modification of one or both of these products. FynT, but not Lck, also associated with c-Cbl in activated T cells. Finally, using a heterologous system, it was demonstrated that the ability of Zap-70 to cause tyrosine phosphorylation of p120c-cbl was dependent on Lck- or FynT-mediated signals. As c-Cbl can associate with several other signaling molecules, it may couple Zap-70 to downstream effectors during T cell activation. |
