Solís, K.H.; Romero-Ávila, M.T.; Rincón-Heredia, R.; García-Sáinz, J.A. Lysophosphatidic Acid Receptor 3 (LPA3): Signaling and Phosphorylation Sites. Preprints2024, 2024040616. https://doi.org/10.20944/preprints202404.0616.v1
APA Style
Solís, K.H., Romero-Ávila, M.T., Rincón-Heredia, R., & García-Sáinz, J.A. (2024). Lysophosphatidic Acid Receptor 3 (LPA3): Signaling and Phosphorylation Sites. Preprints. https://doi.org/10.20944/preprints202404.0616.v1
Chicago/Turabian Style
Solís, K.H., Ruth Rincón-Heredia and J. Adolfo García-Sáinz. 2024 "Lysophosphatidic Acid Receptor 3 (LPA3): Signaling and Phosphorylation Sites" Preprints. https://doi.org/10.20944/preprints202404.0616.v1
Abstract
LPA3 receptors were expressed in TREx HEK 293 cells, and their signaling and phosphorylation were studied. The agonist, lysophosphatidic acid (LPA), increased intracellular calcium and ERK phosphorylation through pertussis toxin-insensitive processes. Phorbol myristate acetate, but not LPA, desensitizes LPA3-mediated calcium signaling. The agonists and the phorbol ester-induced LPA3 internalization. Pitstop 2 (clathrin heavy chain inhibitor) markedly reduced LPA-induced receptor internalization; in contrast, phorbol ester-induced internalization was only delayed. LPA induced rapid β-arrestin-LPA3 receptor association.
The agonist and the phorbol ester induced marked LPA3 receptor phosphorylation, and phosphorylation sites were detected using mass spectrometry. Phosphorylated residues were detected in the intracellular loop 3 (S221, T224, S225, and S229) and in the carboxyl terminus (S321, S325, S331, T333, S335, Y337, and S343). Interestingly, phosphorylation sites are within sequences predicted to constitute β-arrestin binding sites. These data provide insight into LPA3 receptor signaling and regulation.
Medicine and Pharmacology, Pharmacology and Toxicology
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