Alpha and beta subunits of the nicotinic acetylcholine receptor contain covalently bound lipid.
Labeling of the BC3H1 muscle-like cell line with [3H] palmitate, followed by immunoprecipitation of the acetylcholine receptor, indicated that the alpha and beta subunits of the receptor contain covalently bound fatty acid. After acid hydrolysis, fatty acid methyl esters could be recovered from the isolated [3H]palmitate-labeled alpha subunit. Treatment of differentiated BC3H1 cells with cerulenin, an inhibitor of fatty acid and sterol synthesis and fatty acid acylation of proteins, resulted in a 50% inhibition in expression of the acetylcholine receptor on the cell surface under conditions where there was minimal inhibition of protein synthesis. We conclude that this previously undetected post-translational modification may play a role in assembly and/or surface expression of the acetylcholine receptor.
D000818:Animals; D002460:Cell Line; D002569:Cerulenin / Q000494:pharmacology; D005227:Fatty Acids / Q000032:analysis*; D007700:Kinetics; D046911:Macromolecular Substances; D051379:Mice; D008809:Mice, Inbred C3H; D009132:Muscles; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism; D011978:Receptors, Nicotinic / Q000187:drug effects / Q000302:isolation & purification* / Q000378:metabolism
D005227:Fatty Acids; D046911:Macromolecular Substances; D010169:Palmitic Acids; D011978:Receptors, Nicotinic; D002569:Cerulenin; D019308:Palmitic Acid