ArticleThe Journal of experimental medicine1997
RAFTK, a novel member of the focal adhesion kinase family, is phosphorylated and associates with signaling molecules upon activation of mature T lymphocytes.
Article in The Journal of experimental medicine, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 103 citations in OpenAlex.
- The Non-receptor Tyrosine Kinase Pyk2 in Brain Function and Neurological and Psychiatric Diseases.Frontiers in synaptic neuroscience · 2021Review
- Positive and negative regulation by SLP-76/ADAP and Pyk2 of chemokine-stimulated T-lymphocyte adhesion mediated by integrin α4β1.Molecular biology of the cell · 2015Article
- Functions of the FAK family kinases in T cells: beyond actin cytoskeletal rearrangement.Immunologic research · 2014Review
- Eph/ephrin signaling in cell-cell and cell-substrate adhesion.Frontiers in bioscience (Landmark edition) · 2012Review
- Differential expression of FAK and Pyk2 in metastatic and non-metastatic EL4 lymphoma cell lines.Clinical & experimental metastasis · 2011Article
- Regulation of the tyrosine kinase Pyk2 by calcium is through production of reactive oxygen species in cytotoxic T lymphocytes.The Journal of biological chemistry · 2010Article
- Proline-rich tyrosine kinase-2 is critical for CD8 T-cell short-lived effector fate.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Functional activation of proline-rich tyrosine kinase2 (PYK2) in peripheral blood mononuclear cells from patients with systemic lupus erythematosus.BMC musculoskeletal disorders · 2009Article
- The p110delta isoform of PI 3-kinase negatively controls RhoA and PTEN.The EMBO journal · 2007Article
- Focal adhesion kinase-related protein tyrosine kinase Pyk2 in T-cell activation and function.Immunologic research · 2005Review
- Key role of proline-rich tyrosine kinase 2 in interleukin-8 (CXCL8/IL-8)-mediated human neutrophil chemotaxis.Immunology · 2004Article
- Critical role of the carboxyl terminus of proline-rich tyrosine kinase (Pyk2) in the activation of human neutrophils by tumor necrosis factor: separation of signals for the respiratory burst and degranulation.The Journal of experimental medicine · 2003Article
- A PAK1-PIX-PKL complex is activated by the T-cell receptor independent of Nck, Slp-76 and LAT.The EMBO journal · 2001Article
- The tyrosine kinase PYK-2/RAFTK regulates natural killer (NK) cell cytotoxic response, and is translocated and activated upon specific target cell recognition and killing.The Journal of cell biology · 2000Article
- Involvement of proline-rich tyrosine kinase 2 in platelet activation: tyrosine phosphorylation mostly dependent on alphaIIbbeta3 integrin and protein kinase C, translocation to the cytoskeleton and association with Shc through Grb2.The Biochemical journal · 2000Article
- Focal adhesion kinase functions as a receptor-proximal signaling component required for directed cell migration.Immunologic research · 2000Review
- Role of the tyrosine kinase pyk2 in the integrin-dependent activation of human neutrophils by TNF.The Journal of clinical investigation · 1999Article
- The interaction of activated integrin lymphocyte function-associated antigen 1 with ligand intercellular adhesion molecule 1 induces activation and redistribution of focal adhesion kinase and proline-rich tyrosine kinase 2 in T lymphocytes.Molecular biology of the cell · 1999Article
- Separation and characterization of the activated pool of colony-stimulating factor 1 receptor forming distinct multimeric complexes with signalling molecules in macrophages.Molecular and cellular biology · 1999Article
- Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK- cell migration.The EMBO journal · 1998Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The related adhesion focal tyrosine kinase (RAFTK), a recently discovered member of the focal adhesion kinase family, has previously been reported to participate in signal transduction in neuronal cells, megakaryocytes, and B lymphocytes. We have found that RAFTK is constitutively expressed in human T cells and is rapidly phosphorylated upon the activation of the T cell receptor (TCR). This activation also results in an increase in the autophosphorylation and kinase activity of RAFTK. After its stimulation, there was an increase in the association of the src cytoplasmic tyrosine kinase Fyn and the adapter protein Grb2. This association was mediated through the SH2 domains of Fyn and Grb2. RAFTK also co-immunoprecipitates with the SH2 domain of Lck and with the cytoskeletal protein paxillin through its COOH-terminal proline-rich domain. The tyrosine phosphorylation of RAFTK after T cell receptor-mediated stimulation was reduced by the pretreatment of cells with cytochalasin D, suggesting the role of the cytoskeleton in this process. These observations indicate that RAFTK participates in T cell receptor signaling and may act to link signals from the cell surface to the cytoskeleton and thereby affect the host immune response.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.