Dataset for: FFA4 activation induces LPA1 desensitization independent of LPA1 internalization and of FFA4-LPA1 heterodimerization

HEK 293 cells co-expressing fluorescent protein-tagged FFA4 and LPA1 receptors were used to explore LPA1 desensitization. FFA4 activation induced functional desensitization of LPA1 receptors (calcium signaling and ERK 1/2 phosphorylation) and phosphorylation of both FFA4 and LPA1. LPA1 activation induced phosphorylation of LPA1, but not of FFA4 and induced internalization of both receptors into heterogeneous types of vesicles. Interestingly, DHA induced internalization of FFA4 but not of LPA1. Evidence for fatty acid-induced FFA4-LPA1 interaction was obtained by both Förster resonance energy transfer and co-immunoprecipitation studies. Such interaction took place after desensitization was already established. Data indicate that FFA4 activation induces LPA1 desensitization in an internalization-independent process and that complex cellular processes participate in the crosstalk of these receptors.