α and β subunits of the nicotinic acetylcholine receptor contain covalently bound lipid

E. N. Olson, L. Glaser, J. P. Merlie

Research output: Contribution to journalArticle

65 Scopus citations

Abstract

Labeling of the BC3H1 muscle-like cell line with [3H]palmitate, followed by immunoprecipitation of the acetylcholine receptor, indicated that the α and β 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 α 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.

Original languageEnglish (US)
Pages (from-to)5364-5367
Number of pages4
JournalJournal of Biological Chemistry
Volume259
Issue number9
StatePublished - Jan 1 1984

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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