NDLI: cAMP-dependent protein kinase phosphorylates the nicotinic acetylcholine receptor.

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cAMP-dependent protein kinase phosphorylates the nicotinic acetylcholine receptor.

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cAMP-dependent protein kinase phosphorylates the nicotinic acetylcholine receptor.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Greengard, P. Huganir, R. L.
Abstract	Postsynaptic membranes, rich in the nicotinic acetylcholine receptor, were isolated from the electric organ of Torpedo californica and shown to contain a cAMP-dependent protein kinase and a calcium/calmodulin-dependent protein kinase. The cAMP-dependent protein kinase phosphorylated the gamma and delta subunits of the acetylcholine receptor. The phosphorylated subunits were identified after purification of the acetylcholine receptor by affinity chromatography on a choline carboxymethyl affinity gel. In contrast, the calcium/calmodulin-dependent protein kinase phosphorylated proteins that were separated from the acetylcholine receptor by affinity chromatography. Protein kinase inhibitor, a specific inhibitor of the catalytic subunit of cAMP-dependent protein kinase, abolished the basal endogenous phosphorylation of the gamma and delta subunits of the receptor. cAMP activation of the endogenous phosphorylation of the gamma and delta subunits was dose dependent with a half-maximal response at 25 nM. Studies were also carried out with acetylcholine receptor purified from T. californica and catalytic subunit of cAMP-dependent protein kinase purified from bovine heart. The purified acetylcholine receptor was rapidly and specifically phosphorylated on the gamma and delta subunits by the purified catalytic subunit of cAMP-dependent protein kinase to a stoichiometry of 1.0 and 0.89 mol of (32)P per mol of receptor, respectively. The initial rates of phosphorylation of the gamma and delta subunits of the receptor were comparable to those of histone f2B and synapsin I (protein I), two of the most effective substrates for the catalytic subunit. Under the conditions used, the gamma and delta subunits had K(m) values of 4.0 and 3.3 muM and V(max) values of 2.7 and 2.1 mumol/min per mg, respectively. The results are consistent with the idea that the acetylcholine receptor is phosphorylated in vivo by a cAMP-dependent protein kinase.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	80
Language	English
Publisher	National Academy of Sciences
Publisher Date	1983-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Protein Kinases Metabolism Receptors, Cholinergic Receptors, Nicotinic Animals Calcium Calmodulin Cyclic AMP Macromolecular Substances Molecular Weight Phosphoproteins Phosphorylation Torpedo Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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