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Dual regulation by G proteins of agonist‐dependent phosphorylation of muscarinic acetylcholine receptors
Author(s) -
Haga Kazuko,
Haga Tatsuya
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80968-o
Subject(s) - muscarinic acetylcholine receptor , muscarinic acetylcholine receptor m5 , chemistry , muscarinic acetylcholine receptor m1 , phosphorylation , muscarinic acetylcholine receptor m2 , agonist , receptor , muscarinic acetylcholine receptor m3 , g protein , muscarinic acetylcholine receptor m4 , biochemistry
Muscarinic acetylcholine receptors purified from porcine atrium were phosphorylated, depending on the presence of agonists, by a protein kinase partially purified from porcine brain, which had similar properties to the β‐adrenergic receptor kinase. GTP‐binding regulatory proteins (Go) had dual effects on the phosphorylation of muscarinic receptors, i.e. stimulation at lower concentrations and inhibition at higher concentrations. The stimulatory effect was reproduced with the βγ subunit of Go and the inhibitory effect with the combination of the α and βγ subunits.