biostudies-literatureUnknown8Arbulo-Echevarria MMConsejería de Salud, Junta de AndalucíaThe 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-medFrontiers in cell and developmental biology561503https://www.ebi.ac.uk/biostudies/studies/S-EPMC7517355biostudies-literatureIncreased Protein Stability and Interleukin-2 Production of a LAT^G131D Variant With Possible Implications for T Cell Anergy.PMC7517355Vico-Barranco INarbona-Sanchez IMiazek AAguado EGarcia-Cozar FArbulo-Echevarria MMfalseIncreased Protein Stability and Interleukin-2 Production of a LAT^G131D Variant With Possible Implications for T Cell Anergy.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-med2020-01-01T00:00:00Z20202025-05-18T11:49:29.21Z2025-05-18T11:49:29.21ZS-EPMC75173553304299510.3389/fcell.2020.561503