Phosphorylation of brain muscarinic receptor: evidence of receptor regulation.
Muscarinic receptor, from porcine synaptic membrane, was purified by affinity chromatography. Molecular weight analysis by SDS-gel electrophoresis revealed one major peptide with an apparent Mr of 68 +/- 2 Kda. The purified receptor was phosphorylated by the catalytic subunit of cAMP-dependent protein kinase resulting in a concomitant loss in specific binding, and this loss was reversed by calcineurin.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001923:Brain Chemistry; D002118:Calcium / Q000494:pharmacology; D002147:Calmodulin / Q000494:pharmacology; D002148:Calmodulin-Binding Proteins / Q000494:pharmacology; D000242:Cyclic AMP / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D010766:Phosphorylation; D011438:Propylbenzilylcholine Mustard / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D011813:Quinuclidinyl Benzilate / Q000378:metabolism; D011976:Receptors, Muscarinic / Q000378:metabolism*; D013552:Swine; D013570:Synaptic Membranes / Q000032:analysis*
D002147:Calmodulin; D002148:Calmodulin-Binding Proteins; D011976:Receptors, Muscarinic; D011438:Propylbenzilylcholine Mustard; D011813:Quinuclidinyl Benzilate; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D011494:Protein Kinases; D002118:Calcium