Dynamic palmitoylation events following T-cell receptor signaling.

Communications biology (2020-07-12)
Eliot Morrison, Tatjana Wegner, Andres Ernesto Zucchetti, Miguel Álvaro-Benito, Ashley Zheng, Stefanie Kliche, Eberhard Krause, Britta Brügger, Claire Hivroz, Christian Freund

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.

Product Number
Product Description

Monoclonal ANTI-FLAG® M2 antibody produced in mouse, clone M2, purified immunoglobulin (Purified IgG1 subclass), buffered aqueous solution (10 mM sodium phosphate, 150 mM NaCl, pH 7.4, containing 0.02% sodium azide)
Tris[(1-benzyl-1H-1,2,3-triazol-4-yl)methyl]amine, 97%
Saponin Quillaja sp., Sapogenin content 20-35 %
4,4,4-Trifluoro-1-(2-naphthyl)-1,3-butanedione, 99%