Abstract
The temperature sensitivity of nicotinic acetylcholine receptors (AChRs) from T. californica was used to identify steps in AChR subunit folding and oligomerization. Assembly intermediates were isolated by lowering to an assembly-permissive temperature. The earliest identifiable assembly intermediates, αβγ trimers, form minutes after subunit synthesis. αβγδ tetramers are formed slowly by the addition of δ subunits to trimers, and finally a second α subunit is added to form α 2 βγδ pentamers. Between these oligomerization steps, subunits fold as monitored by α-bungarotoxinbinding site formation, appearance of antigenic epitopes, changes in apparent molecular weight, and changes in detergent solubility. Subunit folding requires specific combinations of subunits and correlates in time with subunit additions, suggesting that these subunit folding events contribute to subunit recognition site formation during assembly.
Published Version
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