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Phosphorylation by Cyclic AMP‐Dependent Protein Kinase Modulates Agonist Binding to the D 2 Dopamine Receptor
Author(s) -
Elazar Zvulun,
Fuchs Sara
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb02564.x
Subject(s) - protein kinase a , interleukin 13 receptor , agonist , biochemistry , chemistry , enzyme linked receptor , dopamine receptor d1 , phosphorylation , biology , receptor , microbiology and biotechnology , insulin like growth factor 1 receptor , growth factor
Phosphorylation of striatal membranes by cyclic AMP‐dependent protein kinase resulted in a reduction in the affinity of the D 2 dopamine receptor toward its agonist N ‐propylnorapomorphine while the affinity to D 2 ‐specific antagonists remained unchanged. The inhibitory effects observed by phosphorylation and guanine nucleotides on agonist binding to the D 2 receptor were additive. The purified D 2 dopamine receptor from bovine striatum was specifically phosphorylated by cyclic AMP‐dependent protein kinase with an apparent stoichiometry of 0.7 mol phosphate/mol receptor. The phosphorylated purified D 2 receptor also exhibited a reduced agonist binding activity with no change in antagonist binding. The action of cyclic AMP‐dependent protein kinase on both the membrane preparation and the purified D 2 receptor was inhibited by a specific inhibitor of the kinase. These data indicate that phosphorylation mediated by cyclic AMP‐dependent protein kinase may represent a physiological pathway for modulation of the receptor binding activity.