scholarly journals Dynamic Palmitoylation Events Following T-Cell Receptor Signaling

2019 ◽  
Author(s):  
Eliot Morrison ◽  
Tatjana Wegner ◽  
Andres Ernesto Zucchetti ◽  
Miguel Álvaro-Benito ◽  
Ashley Zheng ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Cell Receptor ◽  
Tcr Signaling ◽  
Reversible Addition ◽  
T Cell Receptor Signaling ◽  
Palmitoyl Acyltransferase ◽  
Ras Signal Transduction ◽  
Cell Receptor Signaling ◽  
Stimulation Of

AbstractPalmitoylation 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.

scholarly journals Dynamic palmitoylation events following T-cell receptor signaling

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Eliot Morrison ◽  
Tatjana Wegner ◽  
Andres Ernesto Zucchetti ◽  
Miguel Álvaro-Benito ◽  
Ashley Zheng ◽  
...  
Keyword(s):  
Signal Transduction ◽  
T Cell ◽  
T Cell Receptor ◽  
T Cell Activation ◽  
Cell Activation ◽  
Cell Receptor ◽  
Receptor Signaling ◽  
Tcr Signaling ◽  
T Cell Receptor Signaling ◽  
Cell Receptor Signaling

AbstractPalmitoylation 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.

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