{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["8"],"submitter":["Arbulo-Echevarria MM"],"funding":["Consejería de Salud, Junta de Andalucía"],"pubmed_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<sup>G131D</sup>) increases phosphorylation of Tyr132, PLC-γ activation and calcium influx generation. Interestingly, the LAT<sup>G131D</sup> mutant has a slower protein turnover while being equally sensitive to Fas-med"],"journal":["Frontiers in cell and developmental biology"],"pagination":["561503"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7517355"],"repository":["biostudies-literature"],"pubmed_title":["Increased Protein Stability and Interleukin-2 Production of a LAT<sup>G131D</sup> Variant With Possible Implications for T Cell Anergy."],"pmcid":["PMC7517355"],"pubmed_authors":["Vico-Barranco I","Narbona-Sanchez I","Miazek A","Aguado E","Garcia-Cozar F","Arbulo-Echevarria MM"],"additional_accession":[]},"is_claimable":false,"name":"Increased Protein Stability and Interleukin-2 Production of a LAT<sup>G131D</sup> Variant With Possible Implications for T Cell Anergy.","description":"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<sup>G131D</sup>) increases phosphorylation of Tyr132, PLC-γ activation and calcium influx generation. Interestingly, the LAT<sup>G131D</sup> mutant has a slower protein turnover while being equally sensitive to Fas-med","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020","modification":"2025-05-18T11:49:29.21Z","creation":"2025-05-18T11:49:29.21Z"},"accession":"S-EPMC7517355","cross_references":{"pubmed":["33042995"],"doi":["10.3389/fcell.2020.561503"]}}