ArticleMolecular and cellular biology1992
Activated lck tyrosine protein kinase stimulates antigen-independent interleukin-2 production in T cells.
Article in Molecular and cellular biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 57 citations in OpenAlex.
- TCRζ-driven pre-signaling organization of Lck in Rab11⁺ endosomes shapes TCR activation.Cellular & molecular biology letters · 2026Article
- Article
- Naturally Occurring Genetic Alterations in Proximal TCR Signaling and Implications for Cancer Immunotherapy.Frontiers in immunology · 2021Review
- Engineering a Dual Small Molecule Gated ZAP70 Switch in T Cells.ACS synthetic biology · 2018Article
- Differential T-cell antigen receptor signaling mediated by the Src family kinases Lck and Fyn.Molecular and cellular biology · 2000Article
- Enhancement of lymphocyte responsiveness by a gain-of-function mutation of ZAP-70.Molecular and cellular biology · 1996Article
- Distinct tyrosine phosphorylation sites in ZAP-70 mediate activation and negative regulation of antigen receptor function.Molecular and cellular biology · 1996Article
- A herpesvirus saimiri membrane protein required for interleukin-2 independence forms a stable complex with p56lck.Journal of virology · 1996Article
- Palmitoylation of either Cys-3 or Cys-5 is required for the biological activity of the Lck tyrosine protein kinase.Molecular and cellular biology · 1995Article
- A general strategy for producing conditional alleles of Src-like tyrosine kinases.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Differential activation of proliferation and cytotoxicity in human T-cell lymphotropic virus type I Tax-specific CD8 T cells by an altered peptide ligand.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Multisubunit receptors in the immune system and their association with the cytoskeleton: in search of functional significance.Immunologic research · 1995Review
- The protein tyrosine kinase p56lck regulates cell adhesion mediated by CD4 and major histocompatibility complex class II proteins.The Journal of experimental medicine · 1994Article
- Protein tyrosine kinase p56-Lck regulates lymphocyte function-associated 1 adhesion molecule expression, granule exocytosis, and cytolytic effector function in a cloned T cell.The Journal of experimental medicine · 1994Article
- Delineation of a T-cell activation motif required for binding of protein tyrosine kinases containing tandem SH2 domains.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- p56lck interacts via its src homology 2 domain with the ZAP-70 kinase.The Journal of experimental medicine · 1994Article
- Oncogenic activation of the Lck protein accompanies translocation of the LCK gene in the human HSB2 T-cell leukemia.Molecular and cellular biology · 1994Article
- Tyrosine phosphorylation of CD45 phosphotyrosine phosphatase by p50csk kinase creates a binding site for p56lck tyrosine kinase and activates the phosphatase.Molecular and cellular biology · 1994Article
- Phosphatidylinositol (PI) 3-kinase and PI 4-kinase binding to the CD4-p56lck complex: the p56lck SH3 domain binds to PI 3-kinase but not PI 4-kinase.Molecular and cellular biology · 1993Article
- Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases.Molecular and cellular biology · 1993Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
p56lck, a member of the src family of cytoplasmic tyrosine kinases, is expressed predominantly in T cells where it associates with the T-cell surface molecules CD4 and CD8. Mutants of CD4 and CD8 that have lost the ability to associate with p56lck no longer enhance antigen-induced T-cell activation. This suggests that p56lck plays an important role during T-cell activation. In an effort to understand the function of p56lck in T cells, a constitutively activated lck gene (F505lck) was introduced into T-helper hybridoma cell lines by retroviral infection. In four T-cell lines we examined, the activated lck protein stimulated interleukin-2 (IL-2) production, a hallmark of T-cell activation, in the absence of antigenic stimulation. In addition, a marked increase in antigen-independent IL-2 production was apparent when T cells infected with a temperature-sensitive F505lck were shifted to the permissive temperature. Only one cell line expressing F505lck exhibited increased sensitivity to antigenic stimulation. The SH3 domain of p56lck was dispensable for the induction of antigen-independent IL-2 production. In contrast, deletion of the majority of the SH2 domain of p56F505lck reduced its ability to induce spontaneous IL-2 production markedly. Activated p60c-src also induced antigen-independent IL-2 production, whereas two other tyrosine kinases, v-abl and the platelet-derived growth factor receptor, did not. Tyrosine phosphorylation of a 70-kDa cellular protein was observed after cross-linking of CD4 in T cells expressing F505lck but not in cells expressing F527src.
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