Mutation of the glycine residue preceding the sixth tyrosine of the LAT adaptor severely alters T cell development and activation.

ABSTRACT: The LAT transmembrane adaptor is essential to transduce intracellular signals triggered by the TCR. Phosphorylation of its four C-terminal tyrosine residues (136, 175, 195, and 235 in mouse LAT) recruits several proteins resulting in the assembly of the LAT signalosome. Among those tyrosine residues, the one found at position 136 of mouse LAT plays a critical role for T cell development and activation. The kinetics of phosphorylation of this residue is delayed as compared to the three other C-terminal tyrosines due to a conserved glycine residue found at position 135. Mutation of this glycine into an aspartate residue (denoted LAT^G135D) increased TCR signaling and altered antigen recognition in human Jurkat T cells and ex vivo mouse T cells. Here, using a strain of LAT^G135D

SUBMITTER: Arbulo-Echevarria MM 

PROVIDER: S-EPMC9768323 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature