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Carboxyl terminus of delta opioid receptor is required for agonist-dependent receptor phosphorylation


Carboxyl terminus of delta opioid receptor is required for agonist-dependent receptor phosphorylation



Biochemical and Biophysical Research Communications 238(1): 71-76



ISSN/ISBN: 0006-291X

PMID: 9299454

DOI: 10.1006/bbrc.1997.7242

The wild-type delta opioid receptor (DOR) and a carboxyl terminus-truncated mutant DOR lacking the last 31 amino acids (DOR-T) were expressed in neuroblastoma x glioma hybrid NG108-15 cells to investigate the role of the carboxyl terminus of DOR in agonist-dependent receptor phosphorylation. Stimulation of the cells with delta specific agonists significantly induced DOR phosphorylation whereas no phosphorylation of DOR-T was detected under the same conditions. Neither overexpression of G protein-coupled receptor kinases (GRK2 or GRK5) nor activation of protein kinase C promoted agonist-induced phosphorylation of DOR-T, in contrast to their strong stimulatory effect on the agonist-dependent phosphorylation of DOR. Furthermore, DOR-T failed to be internalized after agonist stimulation, probably due to its inability to be phosphorylated. Our results indicate that the carboxyl terminus of DOR is required for agonist-dependent receptor phosphorylation and the phosphorylation site(s) of DOR is likely located at its carboxyl terminus.

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Accession: 008264148

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