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Phosphorylation by Protein Kinase C of the Muscarinic Acetylcholine Receptor
Author(s) -
Haga Kazuko,
Haga Tatsuya,
Ichiyama Arata
Publication year - 1990
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.1471-4159.1990.tb01216.x
Subject(s) - muscarinic acetylcholine receptor m5 , muscarinic acetylcholine receptor , muscarinic acetylcholine receptor m3 , muscarinic acetylcholine receptor m2 , phosphorylation , biochemistry , muscarinic acetylcholine receptor m1 , acetylcholine , muscarinic acetylcholine receptor m4 , gtp' , chemistry , biology , receptor , endocrinology , enzyme
Muscarinic acetylcholine receptors purified from porcine cerebrum were phosphorylated by protein kinase C purified from the same tissue. More than 1 mol of phosphate was incorporated per mole of receptor, with both serine and threonine residues being phosphorylated. Neither the degree nor the rate of the phosphorylation was affected by the presence or absence of acetylcholine. GTP‐sensitive high‐affinity binding with acetylcholine was observed for muscarinic receptors reconstituted with GTP‐binding proteins (G i or G o ), irrespective of whether muscarinic receptors or the GTP‐binding proteins had been phosphorylated by protein kinase C or not. This indicates that the interaction between purified muscarinic receptors and purified GTP‐binding proteins in vitro is not affected by their phosphorylation.