A Ser/Thr cluster within the C-terminal domain of the rat prostaglandin receptor EP3 alpha is essential for agonist-induced phosphorylation, desensitization and internalization
Neuschaefer-Rube, F.; Hermosilla, R.; Kuna, M.; Pathe-Neuschaefer-Rube, A.; Schuelein, R.; Pueschel, G.-Paul
British Journal of Pharmacology 145(8): 1132-1142
1 Two isoforms of the rat prostaglandin E-2 receptor, rEP3 alpha-R and rEP3 beta-R, differ only in their C-terminal domain. To analyze the function of the rEP3-R C-terminal domain in agonist induced desensitization, a cluster of Ser/Thr residues in the C-terminal domain of the rEP3 alpha-R was mutated to Ala and both isoforms and the receptor mutant (rEP3 alpha-ST341-349A-R) were stably expressed in HEK293 cells.2 All rEP3-R receptors showed a similar ligand-binding profile.