LPA₃ Receptor Phosphorylation Sites: Roles in Signaling and Internalization.

ABSTRACT: Lysophosphatidic acid (LPA) type 3 (LPA₃) receptor mutants were generated in which the sites detected phosphorylated were substituted by non-phosphorylatable amino acids. Substitutions were made in the intracellular loop 3 (IL3 mutant), the carboxyl terminus (Ctail), and both domains (IL3/Ctail). The wild-type (WT) receptor and the mutants were expressed in T-REx HEK293 cells, and the consequences of the substitutions were analyzed employing different functional parameters. Agonist- and LPA-mediated receptor phosphorylation was diminished in the IL3 and Ctail mutants and essentially abolished in the IL3/Ctail mutant, confirming that the main phosphorylation sites are present in both domains and their role in receptor phosphorylation eliminated by substitution and distributed in

SUBMITTER: Solis KH 

PROVIDER: S-EPMC11122405 | biostudies-literature | 2024 May

REPOSITORIES: biostudies-literature