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The Journal of Neuroscience, August 1, 1999, 19(15):6298-6308

Nicotinic Receptor Assembly Requires Multiple Regions throughout the  Subunit

Alison L. Eertmoed and William N. Green

Department of Pharmacological and Physiological Sciences, University of Chicago, Chicago, Illinois 60637

Assembly of ionotropic neurotransmitter receptors typified by acetylcholine receptors (AChRs) is thought to be directed by an N-terminal extracellular domain of a subunit. Consistent with this hypothesis, chimeras with the  subunit N-terminal domain fused to the rest of the  subunit can substitute for , but not , subunits during AChR assembly. However, chimeras with the  subunit N-terminal domain fused to the rest of the  subunit cannot substitute for  or  subunits during assembly. Furthermore, expression of this chimera with the four wild-type subunits prevents the formation of -bungarotoxin (Bgt) binding sites. Instead of AChR pentamers, complexes are assembled containing only the chimera and either  or  subunits. Based on the results of additional - chimeras, there are at least two different regions within the C-terminal half of the chimera required for the dominant-negative effect. Our results indicate that the N-terminal domain of the  subunit mediates the initial subunit associations, whereas signals in the C-terminal half of the subunit are required for subsequent subunit interactions.

Key words: protein folding; conformational changes; assembly; acetylcholine; -bungarotoxin; nicotinic receptors

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Copyright © 1999 Society for Neuroscience  0270-6474/99/19156298-11$05.00/0

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