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• W2911204792 abstract "The chemokine receptor CCR7 guides T cells and dendritic cells to and within lymph nodes to launch the onset of adaptive immunity. Here, we demonstrate that CCR7 in addition acts as a potent co-stimulatory molecule in T cell activation. We found that antigen recognition and engagement of the TCR results in CCR7 accumulation at the immunological synapse where CCR7 and the TCR co-localize within sub-synaptic vesicles. We demonstrate that CCR7 triggering alone is sufficient to recruit and activate ZAP70, a critical kinase for T cell activation, through Src kinase, whereas TCR CCR7 co-stimulation results in increased and prolonged ZAP70 kinase activity. Finally, we show that ZAP70, acting as adapter molecule, is critical for CCR7-mediated inside-out signaling to integrins, thereby modulating LFA-1 valency regulation to promote cell adhesion, a key step in immunological synapse formation and efficient T cell activation." @default.
• W2911204792 created "2019-01-25" @default.
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• W2911204792 date "2019-01-14" @default.
• W2911204792 modified "2023-09-26" @default.
• W2911204792 title "CCR7 Is Recruited to the Immunological Synapse, Acts as Co-stimulatory Molecule and Drives LFA-1 Clustering for Efficient T Cell Adhesion Through ZAP70" @default.
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• W2911204792 doi "https://doi.org/10.3389/fimmu.2018.03115" @default.
• W2911204792 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6339918" @default.
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• W2911204792 hasPublicationYear "2019" @default.
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