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J. Cell Biol., Volume 146, Number 1, July 12, 1999 203-218
Copyright © 1999 by The Rockefeller University Press.

{alpha}-Bungarotoxin Receptors Contain {alpha}7 Subunits in Two Different Disulfide-bonded Conformations

Sergey Rakhilin, Renaldo C. Drisdel, Daphna Sagher, Daniel S. McGeheea, Yolanda Vallejo, and William N. Green
a Department of Pharmacological and Physiological Sciences, Department of Anesthesia and Critical Care, University of Chicago, Chicago, Illinois 60637

Correspondence to: William N. Green, Department of Pharmacological and Physiological Sciences, University of Chicago, 947 East 58th Street, Chicago, IL 60637., wgreen{at}midway.uchicago.edu (E-mail), (773) 702-1763 (phone), (773) 702-3774 (fax)

Neuronal nicotinic {alpha}7 subunits assemble into cell-surface complexes that neither function nor bind {alpha}-bungarotoxin when expressed in tsA201 cells. Functional {alpha}-bungarotoxin receptors are expressed if the membrane-spanning and cytoplasmic domains of the {alpha}7 subunit are replaced by the homologous regions of the serotonin-3 receptor subunit. Bgt-binding surface receptors assembled from chimeric {alpha}7/serotonin-3 subunits contain subunits in two different conformations as shown by differences in redox state and other features of the subunits. In contrast, {alpha}7 subunit complexes in the same cell line contain subunits in a single conformation. The appearance of a second {alpha}7/serotonin-3 subunit conformation coincides with the formation of {alpha}-bungarotoxin–binding sites and intrasubunit disulfide bonding, apparently within the {alpha}7 domain of the {alpha}7/serotonin-3 chimera. In cell lines of neuronal origin that produce functional {alpha}7 receptors, {alpha}7 subunits undergo a conformational change similar to {alpha}7/serotonin-3 subunits. {alpha}7 subunits, thus, can fold and assemble by two different pathways. Subunits in a single conformation assemble into nonfunctional receptors, or subunits expressed in specialized cells undergo additional processing to produce functional, {alpha}-bungarotoxin–binding receptors with two {alpha}7 conformations. Our results suggest that {alpha}7 subunit diversity can be achieved postranslationally and is required for functional homomeric receptors.

Key Words: {alpha}-bungarotoxin, {alpha}7 subunits, nicotinic receptors, protein folding, disulfide bonds


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