Phosphorylation by protein kinase C modulates agonist binding to striatal dopamine D2 receptors.
The effect of purified protein kinase C (PKC) on dopamine D2 receptor binding was studied. Saturation binding with [3H]spiperone was not affected. In competition experiments using agonists PKC-treated membranes showed a significant reduction in the proportion of high affinity sites, and the influence of GTP gamma S was abolished. These results suggest that PKC-dependent mechanisms can regulate the coupling between the dopamine D2 receptor and its G-protein.
Rogue
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Centre de Neurochimie du C.N.R.S., Strasbourg, France.
Zwiller
J
J
Malviya
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AN
Vincendon
G
G
D000818:Animals; D001667:Binding, Competitive / Q000502:physiology; D002417:Cattle; D003342:Corpus Striatum / Q000378:metabolism*; D015259:Dopamine Agents / Q000378:metabolism*; D066298:In Vitro Techniques; D010766:Phosphorylation; D011493:Protein Kinase C / Q000302:isolation & purification / Q000378:metabolism*; D011869:Radioligand Assay; D011954:Receptors, Dopamine / Q000378:metabolism*; D017448:Receptors, Dopamine D2
D015259:Dopamine Agents; D011954:Receptors, Dopamine; D017448:Receptors, Dopamine D2; D011493:Protein Kinase C