Dynamic palmitoylation events following T-cell receptor signaling

Commun Biol. 2020 Jul 10;3(1):368. doi: 10.1038/s42003-020-1063-5.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / metabolism
  • Animals
  • Fluorescent Antibody Technique
  • Gas Chromatography-Mass Spectrometry
  • Humans
  • Insecta
  • Jurkat Cells / metabolism
  • Lipoylation*
  • R-SNARE Proteins / metabolism
  • Receptors, Antigen, T-Cell / metabolism*
  • Signal Transduction*


  • R-SNARE Proteins
  • Receptors, Antigen, T-Cell
  • VAMP7 protein, human
  • Acyltransferases
  • ZDHHC20 protein, human