| First Author | Zhu X | Year | 1997 |
| Journal | Biochem Biophys Res Commun | Volume | 232 |
| Issue | 2 | Pages | 513-6 |
| PubMed ID | 9125212 | Mgi Jnum | J:38960 |
| Mgi Id | MGI:86346 | Doi | 10.1006/bbrc.1997.6324 |
| Citation | Zhu X, et al. (1997) The carboxyl terminus of mouse delta-opioid receptor is not required for agonist-dependent activation. Biochem Biophys Res Commun 232(2):513-6 |
| abstractText | The pharmacological effects caused by use of opiate are exerted through the opioid receptors (ORs). ORs couple to the inhibitory G protein (Gi) and result in decreased cAMP levels upon activation by specific agonists. To initiate study of the structure-function relationship during this process, we first ectopically expressed the wild-type delta OR and a C-terminally truncated mutant in CHO cells to investigate the necessity of its C-terminus. The binding potency of both the wild-type and truncated delta ORs to ligands including DPDPE, DSLET, DAGO, and U-50488 was compared. Their membrane localization and ability to mediate signal transduction were also studied. We conclude that the C-terminus of delta OR is not essential for plasma membrane targeting, ligand specificity, and agonist-dependent activation. |
