Increased Protein Stability and Interleukin-2 Production of a LAT^G131D Variant With Possible Implications for T Cell Anergy.

ABSTRACT: The adaptor LAT plays a crucial role in the transduction of signals coming from the TCR/CD3 complex. Phosphorylation of some of its tyrosines generates recruitment sites for other cytosolic signaling molecules. Tyrosine 132 in human LAT is essential for PLC-γ activation and calcium influx generation. It has been recently reported that a conserved glycine residue preceding tyrosine 132 decreases its phosphorylation kinetics, which constitutes a mechanism for ligand discrimination. Here we confirm that a LAT mutant in which glycine 131 has been substituted by an aspartate (LAT^G131D) increases phosphorylation of Tyr132, PLC-γ activation and calcium influx generation. Interestingly, the LAT^G131D mutant has a slower protein turnover while being equally sensitive to Fas-med

SUBMITTER: Arbulo-Echevarria MM 

PROVIDER: S-EPMC7517355 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature