Carlin_1986_Proc.Natl.Acad.Sci.U.S.A_83_498

We have identified an intracellular form of the alpha subunit of the acetylcholine receptor that binds alpha-bungarotoxin with high affinity. Unlike the mature receptor complex, an alpha 2 beta gamma delta pentamer that migrates as a 9S species in velocity sedimentation analysis, the intracellular species moves as a 5S component. The kinetics of appearance of alpha subunit in the 5S component and the mature receptor complex indicate that the intracellular 5S component is a precursor of the mature receptor. The precursor species differs from 9S receptor in two critical features: (i) the precursor alpha subunit is not associated with beta subunit and (ii) alpha-bungarotoxin binding to the precursor alpha subunit is not inhibited by the cholinergic ligands decamethonium or d-tubocurarine. The properties of the precursor suggest that the acquisition of the ligand binding site by alpha subunit occurs at a distinct stage in the posttranslational development of functional acetylcholine receptor.