ArticleThe Journal of cell biology1997
ZAP-70 protein tyrosine kinase is constitutively targeted to the T cell cortex independently of its SH2 domains.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 31 citations in OpenAlex.
- Integration of FRET and sequencing to engineer kinase biosensors from mammalian cell libraries.Nature communications · 2021Article
- Positive feedback between the T cell kinase Zap70 and its substrate LAT acts as a clustering-dependent signaling switch.Cell reports · 2021Article
- SH2 Domains Serve as Lipid-Binding Modules for pTyr-Signaling Proteins.Molecular cell · 2016Article
- T cell receptor dwell times control the kinase activity of Zap70.Nature immunology · 2015Article
- Immune synapse formation requires ZAP-70 recruitment by ezrin and CD43 removal by moesin.The Journal of cell biology · 2007Article
- 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
- Involvement of crk adapter proteins in regulation of lymphoid cell functions.Immunologic research · 2003Review
- Genetic evidence for Shc requirement in TCR-induced c-Rel nuclear translocation and IL-2 expression.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Article
- Prolactin receptor signaling: shared components with the T-cell antigen receptor in Nb2 lymphoma cells.Endocrine · 1998Article
- T cell receptor (TCR) engagement in apoptosis-defective, but interleukin 2 (IL-2)-producing, T cells results in impaired ZAP70/CD3-zeta association.The Journal of experimental medicine · 1998Article
- Compartmentalized IgE receptor-mediated signal transduction in living cells.The Journal of cell biology · 1997Article
- Regulation of ZAP-70 intracellular localization: visualization with the green fluorescent protein.The Journal of experimental medicine · 1997Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ZAP-70 is a nonreceptor protein tyrosine kinase that is essential for signaling via the T cell antigen receptor (TCR). ZAP-70 becomes phosphorylated and activated by LCK protein tyrosine kinase after interaction of its two NH2-terminal SH2 domains with tyrosine-phosphorylated subunits of the activated TCR. In this study, the localization of ZAP-70 was investigated by immunofluorescence and confocal microscopy. ZAP-70 was found to be localized to the cell cortex in a diffuse band under the plasma membrane in unstimulated T cells, and this localization was not detectably altered by TCR stimulation. Analysis of mutants indicated that ZAP-70 targeting was independent of its SH2 domains but required its active kinase domain. The specific compartmentalization of ZAP-70 suggests that it may interact with an anchoring protein in the cell cortex via its hinge or kinase domains. It is likely that the maintenance of high concentrations of ZAP-70 at the cell cortex, that only has to move a short distance to interact with phophorylated TCR subunits, facilitates rapid initiation of signaling by the TCR. In addition, as the major increase in tyrosine phosphorylation induced by the TCR also occurs at the cell cortex (Ley, S.C., M. Marsh, C.R. Bebbington, K. Proudfoot, and P. Jordan. 1994. J. Cell. Biol. 125:639-649), ZAP-70 may be localized close to its downstream targets.
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