{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Morrison E"],"funding":["Massachusetts Department of Fish and Game"],"pagination":["368"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7351954"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["3(1)"],"pubmed_abstract":["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. Ce"],"journal":["Communications biology"],"pubmed_title":["Dynamic palmitoylation events following T-cell receptor signaling."],"pmcid":["PMC7351954"],"funding_grant_id":["TRR186"],"pubmed_authors":["Kliche S","Hivroz C","Freund C","Morrison E","Brugger B","Alvaro-Benito M","Krause E","Wegner T","Zheng A","Zucchetti AE"],"additional_accession":[]},"is_claimable":false,"name":"Dynamic palmitoylation events following T-cell receptor signaling.","description":"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. Ce","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jul","modification":"2026-07-15T23:41:23.307Z","creation":"2025-04-05T12:43:45.011Z"},"accession":"S-EPMC7351954","cross_references":{"pubmed":["32651440"],"doi":["10.1038/s42003-020-1063-5"]}}