Dynamic Palmitoylation Events Following T-Cell Receptor Signaling

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-d...

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Published inbioRxiv
Main Authors Morrison, Eliot, Wegner, Tatjana, Zucchetti, Andres Ernesto, Alvaro-Benito, Miguel, Zheng, Ashley, Kliche, Stefanie, Krause, Eberhard, Bruegger, Britta, Hivroz, Claire, Freund, Christian
Format Paper
LanguageEnglish
Published Cold Spring Harbor Cold Spring Harbor Laboratory Press 05.11.2019
Subjects
Acyltransferase
Golgi apparatus
Isoforms
Lymphocytes T
Palmitic acid
Palmitoylation
Signal transduction
SNAP receptors
T cell receptors
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Summary: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.
DOI:10.1101/831388