Abstract:
:Prostaglandin E2 receptors (EPR), which belong to the family of heterotrimeric G protein-coupled ectoreceptors with seven transmembrane domains, can be classified into four subtypes according to their ligand binding and G protein coupling specificity. Of these, EP3betaR is coupled to Gi, whereas EP4R is coupled to Gs. EP4R, in contrast to EP3betaR, shows agonist-induced desensitization. The C-terminal domain and the third intracellular loop of these receptors have been implicated in G protein coupling specificity and desensitization. Here, receptor hybrids consisting of the main portion of rat EP3betaR and either the C-terminal domain or the third intracellular loop of human EP4R were used to study the contribution of the respective receptor domains to G protein coupling and desensitization. Neither the EP4R C-terminal domain nor the EP4R third intracellular loop alone was sufficient to change the coupling specificity of the rEP3hEP4 receptor hybrids from Gi to Gs or to confer additional Gs coupling. However, the EP4R C-terminal domain but not the third intracellular loop was necessary and sufficient to mediate rapid agonist-induced, second messenger-independent desensitization in the Gi-coupled hybrid receptors.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Neuschäfer-Rube F,Hänecke K,Püschel GPdoi
10.1016/s0014-5793(97)01105-8subject
Has Abstractpub_date
1997-09-29 00:00:00pages
119-24issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(97)01105-8journal_volume
415pub_type
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