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J. Biol. Chem., Vol. 259, Issue 9, 5364-5367, 05, 1984
EN Olson, L Glaser and JP Merlie
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.
Alpha and beta subunits of the nicotinic acetylcholine receptor contain covalently bound lipid
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