Journal
COMMUNICATIONS BIOLOGY
Volume 3, Issue 1, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s42003-020-1063-5
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Funding
- DFG [TRR186]
- Institut Curie
- Institut National de la Sante et de la Recherche Medicale (INSERM)
- ANR [ANR-10-IDEX-0001-02 PSL*, ANR-11-LABX-0043]
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Palmitoylation is the reversible addition of palmitate to cysteine via a thioester linkage. The reversible nature of this modification makes it a prime candidate as a mechanism for regulating signal transduction in T-cell receptor signaling. 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 and to localize to the immune synapse upon T cell activation. Morrison et al. find that in T-cells, the palmitoyl acetyltransferase DHHC18 palmitoylates the v-SNARE VAMP7 at Cys183 and show that a mutant that cannot be palmitoylated fails to localise to Golgi and traffic to the immune synapse after T-cell receptor activation. This study highlights the importance of palmitoylation in T-cell signalling.
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