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• W2019428712 startingPage "17896" @default.
• W2019428712 abstract "In T cells, cell surface expression of CD45, a transmembrane tyrosine phosphatase, is required for T cell receptor (TCR) signal transduction. Indirect evidence suggests that CD45 function in TCR signaling involves the dephosphorylation of the C-terminal negative regulatory site of p56lck, Tyr-505. To evaluate the importance of CD45-mediated dephosphorylation of p56lck Tyr-505 in TCR signaling, we established CD45− Jurkat cell lines expressing various forms of a chimera containing the extracellular and transmembrane domains of the epidermal growth factor receptor (EGFR) fused to p56lck. We report that an activated EGFR/Lck chimera is able to reconstitute a Ca2+ response after CD3 stimulation in the absence of CD45 expression. In addition, the wild-type and kinase inactive versions of the EGFR/Lck chimera fail to restore early signaling. Restoration of the response by EGFR/LckF505 required EGF binding to the chimeric kinase. Altogether, these results provide the first direct evidence that the lack of efficient dephosphorylation of p56lck Tyr-505 is, in part, responsible for the unresponsiveness of CD45− cells. They also indicate that a second event is required for p56lck function in TCR signaling in addition to its dephosphorylation at Tyr-505. In T cells, cell surface expression of CD45, a transmembrane tyrosine phosphatase, is required for T cell receptor (TCR) signal transduction. Indirect evidence suggests that CD45 function in TCR signaling involves the dephosphorylation of the C-terminal negative regulatory site of p56lck, Tyr-505. To evaluate the importance of CD45-mediated dephosphorylation of p56lck Tyr-505 in TCR signaling, we established CD45− Jurkat cell lines expressing various forms of a chimera containing the extracellular and transmembrane domains of the epidermal growth factor receptor (EGFR) fused to p56lck. We report that an activated EGFR/Lck chimera is able to reconstitute a Ca2+ response after CD3 stimulation in the absence of CD45 expression. In addition, the wild-type and kinase inactive versions of the EGFR/Lck chimera fail to restore early signaling. Restoration of the response by EGFR/LckF505 required EGF binding to the chimeric kinase. Altogether, these results provide the first direct evidence that the lack of efficient dephosphorylation of p56lck Tyr-505 is, in part, responsible for the unresponsiveness of CD45− cells. They also indicate that a second event is required for p56lck function in TCR signaling in addition to its dephosphorylation at Tyr-505." @default.
• W2019428712 created "2016-06-24" @default.
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• W2019428712 date "1996-07-01" @default.
• W2019428712 modified "2023-10-17" @default.
• W2019428712 title "An Activated Epidermal Growth Factor Receptor/Lck Chimera Restores Early T Cell Receptor-mediated Calcium Response in a CD45-deficient T Cell Line" @default.
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• W2019428712 doi "https://doi.org/10.1074/jbc.271.30.17896" @default.
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