Identification of a Ser/Thr cluster in the C-terminal domain of the human prostaglandin receptor EP4 that is essential for agonist-induced beta-arrestin1 recruitment but differs from the apparent principal phosphorylation site.

@article{NeuschaeferRube2004IdentificationOA,
  title={Identification of a Ser/Thr cluster in the C-terminal domain of the human prostaglandin receptor EP4 that is essential for agonist-induced beta-arrestin1 recruitment but differs from the apparent principal phosphorylation site.},
  author={Frank Neuschaefer-Rube and Ricardo Hermosilla and Mathias Rehwald and Lars R{\"o}nnstrand and Ralf Schuelein and Christer Wernstedt and Gerhard Paul P{\"u}schel},
  journal={The Biochemical journal},
  year={2004},
  volume={379 Pt 3},
  pages={573-85}
}
hEP4-R (human prostaglandin E2 receptor, subtype EP4) is a G(s)-linked heterotrimeric GPCR (G-protein-coupled receptor). It undergoes agonist-induced desensitization and internalization that depend on the presence of its C-terminal domain. Desensitization and internalization of GPCRs are often linked to agonist-induced beta-arrestin complex formation, which is stabilized by phosphorylation. Subsequently beta-arrestin uncouples the receptor from its G-protein and links it to the endocytotic… CONTINUE READING