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PMID: 264679 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Phosphorylation of membrane proteins at a cholinergic synapse.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 74 ·No. 1 ·1977-01-00 ·Pages 263-7

Gordon AS, Davis CG, Diamond I

Abstract

Endogenous membrane protein kinase activity and protein kinase substrates have been found in membrane fractions enriched in the acetylcholine receptor that were prepared from the electric organ of Torpedo californica. Phosphorylation of four polypeptides is stimulated 9-fold by K+. The specific cholinergic ligand, carbachol, inhibited phosphorylation of these four polypeptides by 72% in the presence of 1mM Na+ and 100 mM K+. The 65,000-dalton component of the acetylcholine receptor in the membrane fraction appears to be phosphorylated by the endogenous protein kinase. These results suggest that protein phosphorylation may play an important role in synaptic events at nicotinic cholinergic synapses.

MeSH Terms
Animals Carbachol/pharmacology Electric Organ Fishes Ligands/pharmacology Membrane Proteins/metabolism Molecular Weight Phosphates/metabolism Potassium/metabolism Protein Kinases/metabolism Receptors, Cholinergic/metabolism Receptors, Nicotinic/drug effects,metabolism Sodium/pharmacology Synaptic Membranes/metabolism
Chemicals
Ligands Membrane Proteins Phosphates Receptors, Cholinergic Receptors, Nicotinic Carbachol Sodium Protein Kinases Potassium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Gordon A S
Davis C G
Diamond I
References (33)
33 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.74.1.263
Published
1977-01-00
Pages
263-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC393239
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.74.1.263 PMC Full Text View journal details
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