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Dynamic palmitoylation events following T-cell receptor signaling

Morrison, Eliot and Wegner, Tatjana and Zucchetti, Andres Ernesto and Álvaro-Benito, Miguel – 2020

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.

Title
DynamicPalmitoylation_Morrison
Author
Morrison, Eliot and Wegner, Tatjana and Zucchetti, Andres Ernesto and Álvaro-Benito, Miguel
Date
2020-07-10
Identifier
10.1038/s42003-020-1063-5
Source(s)
Appeared in
Nature Communications Biology - Volume 3, Issue 1, art. Num. 368
Language
eng
Type
Text