Phosphorylated mu-opioid receptor purified from rat brains lacks functional coupling with Gi1, a GTP-binding protein in reconstituted lipid vesicles

H Harada; H Ueda; T Katada; M Ui; M Satoh

doi:10.1016/0304-3940(90)90492-r

Phosphorylated mu-opioid receptor purified from rat brains lacks functional coupling with Gi1, a GTP-binding protein in reconstituted lipid vesicles

Neurosci Lett. 1990 May 18;113(1):47-9. doi: 10.1016/0304-3940(90)90492-r.

Authors

H Harada¹, H Ueda, T Katada, M Ui, M Satoh

Affiliation

¹ Department of Pharmacology, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.

PMID: 2164175
DOI: 10.1016/0304-3940(90)90492-r

Abstract

The effects of phosphorylation of a mu-opioid receptor on signal transduction to G-protein were studied. The mu-opioid receptor purified from rat whole brains was reconstituted with purified Gi1 in phosphatidylcholine vesicles. DAGO, a mu-opioid agonist at 1 microM-1 mM increased GTPase activity by 10-110% of control, in a concentration-dependent manner. When the mu-opioid receptor was phosphorylated by cyclic AMP-dependent protein kinase prior to reconstitution with Gi1, the DAGO-stimulation was markedly reduced (20% increase at 1 mM DAGO).

MeSH terms

Animals
Enkephalin, Ala(2)-MePhe(4)-Gly(5)-
Enkephalins / pharmacology*
GTP-Binding Proteins / metabolism
GTP-Binding Proteins / physiology*
Liposomes
Phosphatidylcholines
Phosphorylation
Rats
Rats, Inbred Strains
Receptors, Opioid / drug effects
Receptors, Opioid / metabolism*
Receptors, Opioid / physiology
Receptors, Opioid, mu
Signal Transduction*

Substances

Enkephalins
Liposomes
Phosphatidylcholines
Receptors, Opioid
Receptors, Opioid, mu
Enkephalin, Ala(2)-MePhe(4)-Gly(5)-
GTP-Binding Proteins