p56lck interacts via its src homology 2 domain with the ZAP-70 kinase
| Autor: | Pascale Duplay, Margot Thome, F Herve, Oreste Acuto |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
CD3 Complex
Immunology Molecular Sequence Data Receptors Antigen T-Cell Sequence Homology chemical and pharmacologic phenomena Protein tyrosine phosphatase Biology SH2 domain Receptor tyrosine kinase SH3 domain Cell Line Immunology and Allergy Humans ZAP-70 Protein-Tyrosine Kinase Base Sequence hemic and immune systems DNA Articles Protein-Tyrosine Kinases Biochemistry Lymphocyte Specific Protein Tyrosine Kinase p56(lck) biology.protein GRB2 Tyrosine kinase Binding domain Proto-oncogene tyrosine-protein kinase Src Signal Transduction |
| Zdroj: | The Journal of Experimental Medicine |
| Popis: | p56lck, a member of the src family of protein tyrosine kinases, is an essential component in T cell receptor (TCR) signal transduction. p56lck contains a src homology 2 (SH2) domain found in a number of proteins involved in intracellular signaling. SH2 domains have been implicated in protein-protein interactions by binding to sequences in target proteins containing phosphorylated tyrosine. Using an in vitro assay, we have studied specific binding of tyrosine-phosphorylated proteins to a recombinant p56lck SH2 domain. In nonactivated Jurkat cells, two tyrosine-phosphorylated proteins were detected. Stimulation with anti-CD3 monoclonal antibodies induced the binding of seven additional tyrosine-phosphorylated proteins to the SH2 domain of p56lck. We have identified the zeta-associated tyrosine kinase, ZAP-70, as one of these proteins. Evidence suggests that binding of ZAP-70 to p56lck SH2 is direct and not mediated by zeta. The significance of this interaction was further investigated in vivo. p56lck could be coprecipitated with the zeta/ZAP-70 complex and conversely, ZAP-70 was detected in p56lck immunoprecipitates of activated Jurkat cells. The physical association of p56lck and ZAP-70 during activation supports the recently proposed functional cooperation of these two tyrosine kinases in TCR signaling. |
| Databáze: | OpenAIRE |
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