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