Molecular Cloning of Receptors for Acetylcholine

Abstract

The nicotinic acetylcholine receptor at the vertebrate neuromuscular junction has provided an excellent model both for studies of ligand-gated ion channels and for studies of neural regulation of the synthesis and properties of constituents of the neuromuscular junction. Research in many laboratories studying the biochemical and biophysical properties of the receptor has led to our current view of the receptor molecule (for review see Cold Spring Harbor Symposium on Quantitative Biology, Vol. XLVIII). The results of this research have also provided the basis for another more recent assault on the structure and regulation of the acetylcholine receptor. In this work the emphasis has been on the isolation of recombinant DNA molecules coding for the polypeptides that comprise the receptor oligomer. The nucleotide sequences of these DNA molecules provided the amino acid sequence of each of the four receptor subunits (Noda et al. 1983) and analysis of these sequences has provided support for various models for the disposition of receptor sequences across the membrane (Claudio et al. 1983) and for the location (Noda et al. 1983) of the acetylcholine binding site.