γ- and δ-subunits regulate the affinity and the cooperativity of ligand binding to the acetylcholine receptor

Steven M Sine, T. Claudio

Research output: Contribution to journalArticle

144 Citations (Scopus)

Abstract

The acetylcholine receptor (AChR) from vertebrate skeletal muscle is a pentamer composed of two ligand-binding α-subunits and one β-, γ-, and δ-subunit. To examine the functional roles of the non-α-subunits, we have expressed, in stable cell lines, AChRs lacking either a γ- or a δ-subunit. Most previous work has examined how these changes in subunit composition affect single channel properties. Here, we take advantage of the stable expression system to produce large amounts of AChR and, for the first time, examine ligand binding to altered AChRs on intact cells. The changes in subunit composition affect both ligand affinity and cooperativity of the receptor, suggesting important roles for the γ- and δ-subunits, both in shaping the ligand binding site and maintaining cooperative interactions between α-subunits.

Original languageEnglish (US)
Pages (from-to)19369-19377
Number of pages9
JournalJournal of Biological Chemistry
Volume266
Issue number29
StatePublished - 1991
Externally publishedYes

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Cholinergic Receptors
Ligands
Chemical analysis
Muscle
Vertebrates
Skeletal Muscle
Binding Sites
Cells
Cell Line

ASJC Scopus subject areas

  • Biochemistry

Cite this

γ- and δ-subunits regulate the affinity and the cooperativity of ligand binding to the acetylcholine receptor. / Sine, Steven M; Claudio, T.

In: Journal of Biological Chemistry, Vol. 266, No. 29, 1991, p. 19369-19377.

Research output: Contribution to journalArticle

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