NDLI: Association of tyrosine protein kinase Zap-70 with the protooncogene product p120c-cbl in T lymphocytes.

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Association of tyrosine protein kinase Zap-70 with the protooncogene product p120c-cbl in T lymphocytes.

Content Provider	Scilit
Author	Fournel, M. Davidson, D. Weil, R. Veillette, A.
Copyright Year	1996
Description	Journal: The Journal of experimental medicine 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.
Related Links	http://jem.rupress.org/content/183/1/301.full.pdf https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2192430/pdf
ISSN	00221295
DOI	10.1084/jem.183.1.301
Journal	The Journal of experimental medicine
Issue Number	1
Volume Number	183
Language	English
Publisher	Rockefeller University Press
Publisher Date	1996-01-01
Access Restriction	Open
Subject Keyword	Journal: The Journal of experimental medicine Phosphorylated Mediated Signal
Content Type	Text
Resource Type	Article
Subject	Physiology

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