bioRxiv · 10.1101/831388
Dynamic Palmitoylation Events Following T-Cell Receptor Signaling
Abstract
Palmitoylation is the reversible addition of palmitate to cysteine via a thioester linkage. Following stimulation of the T-cell receptor we find a number of proteins are newly palmitoylated, including those involved in vesicle-mediated transport and Ras signal transduction. Among these stimulation-dependent palmitoylation targets are the v-SNARE VAMP7, important for docking of vesicular LAT during TCR signaling, and the largely undescribed palmitoyl acyltransferase DHHC18 that is expressed in two isoforms in T cells. Using our newly developed On-Plate Palmitoylation Assay (OPPA), we show DHHC18 is capable of palmitoylating VAMP7 at Cys183. Cellular imaging shows that the palmitoylation-deficient protein fails to be retained at the Golgi.
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Morrison, E., Wegner, T., Zucchetti, A. E., Alvaro-Benito, M., Zheng, A., Kliche, S., Krause, E., Bruegger, B., Hivroz, C., Freund, C.. 2019-11-05. Dynamic Palmitoylation Events Following T-Cell Receptor Signaling. https://doi.org/10.1101/831388
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