ArticleThe Journal of experimental medicine1994
p56lck interacts via its src homology 2 domain with the ZAP-70 kinase.
Article in The Journal of experimental medicine, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 159 citations in OpenAlex.
- HIV Nef disrupts Lck signaling by inducing aberrant phosphorylation of its substrates.ImmunoHorizons · 2025Article
- T-cell virtuosity in ''knowing thyself".Frontiers in immunology · 2024Review
- Cyclophilin A associates with and regulates the activity of ZAP70 in TCR/CD3-stimulated T cells.Cellular and molecular life sciences : CMLS · 2022Article
- Cooperative binding of T cell receptor and CD4 to peptide-MHC enhances antigen sensitivity.Nature communications · 2022Article
- T cell receptor (TCR) signaling in health and disease.Signal transduction and targeted therapy · 2021Review
- PD-1 suppresses TCR-CD8 cooperativity during T-cell antigen recognition.Nature communications · 2021Article
- Potential of nintedanib in treatment of progressive fibrosing interstitial lung diseases.The European respiratory journal · 2019Review
- How does the kinase Lck phosphorylate the T cell receptor? Spatial organization as a regulatory mechanism.Frontiers in immunology · 2012Article
- ZAP70: a master regulator of adaptive immunity.Seminars in immunopathology · 2010Review
- Spatial differences in active caspase-8 defines its role in T-cell activation versus cell death.Cell death and differentiation · 2008Article
- Carcinoembryonic antigen-related cell adhesion molecule 1 inhibits proximal TCR signaling by targeting ZAP-70.Journal of immunology (Baltimore, Md. : 1950) · 2008Article
- Lck SH3 domain function is required for T-cell receptor signals regulating thymocyte development.Molecular and cellular biology · 2006Article
- Critical role of Ser-520 phosphorylation for membrane recruitment and activation of the ZAP-70 tyrosine kinase in T cells.Molecular and cellular biology · 2003Article
- Positive and negative regulation of T-cell activation through kinases and phosphatases.The Biochemical journal · 2003Review
- T cell development and T cell responses in mice with mutations affecting tyrosines 292 or 315 of the ZAP-70 protein tyrosine kinase.The Journal of experimental medicine · 2001Article
- Constitutive activation of the Ras/MAP kinase pathway and enhanced TCR signaling by targeting the Shc adaptor to membrane rafts.Oncogene · 2000Article
- Differential T-cell antigen receptor signaling mediated by the Src family kinases Lck and Fyn.Molecular and cellular biology · 2000Article
- Functional analysis of H-Ryk, an atypical member of the receptor tyrosine kinase family.Molecular and cellular biology · 1999Article
- ZAP-70 protein promotes tyrosine phosphorylation of T cell receptor signaling motifs (ITAMs) in immature CD4(+)8(+) thymocytes with limiting p56(lck).The Journal of experimental medicine · 1999Article
- Prolactin receptor signaling: shared components with the T-cell antigen receptor in Nb2 lymphoma cells.Endocrine · 1998Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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