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- W2892280916 abstract "Upon engagement of the T cell receptor with an antigen-presenting cell, LCK initiates TCR signaling by phosphorylating its activation motifs. However, the mechanism of LCK activation specifically at the immune synapse is a major question. We show that phosphorylation of the LCK activating Y394, despite modestly increasing its catalytic rate, dramatically focuses LCK localization to the immune synapse. We describe a trafficking mechanism whereby UNC119A extracts membrane-bound LCK by sequestering the hydrophobic myristoyl group, followed by release at the target membrane under the control of the ciliary ARL3/ARL13B. The UNC119A N terminus acts as a “regulatory arm” by binding the LCK kinase domain, an interaction inhibited by LCK Y394 phosphorylation, thus together with the ARL3/ARL13B machinery ensuring immune synapse focusing of active LCK. We propose that the ciliary machinery has been repurposed by T cells to generate and maintain polarized segregation of signals such as activated LCK at the immune synapse." @default.
- W2892280916 created "2018-09-27" @default.
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- W2892280916 date "2018-10-01" @default.
- W2892280916 modified "2023-10-10" @default.
- W2892280916 title "The Ciliary Machinery Is Repurposed for T Cell Immune Synapse Trafficking of LCK" @default.
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- W2892280916 doi "https://doi.org/10.1016/j.devcel.2018.08.012" @default.
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