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Volume 271, Number 27, Issue of July 5, 1996 pp. 16035-16039
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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An Amino Acid Substitution in the Pore Region of a Glutamate-gated Chloride Channel Enables the Coupling of Ligand Binding to Channel Gating

(Received for publication, January 26, 1996, and in revised form, April 16, 1996)

Adrian Etter , Doris F. Cully , James M. Schaeffer , Ken K. Liu and Joseph P. Arena

From the Merck Research Laboratories, Department of Cell Biochemistry and Physiology,  Department of Genetics and Molecular Biology, Rahway, New Jersey 07065-0900

Many of the subunits of ligand-gated ion channels respond poorly, if at all, when expressed as homomeric channels in Xenopus oocytes. This lack of a ligand response has been thought to result from poor surface expression, poor assembly, or lack of an agonist binding domain. The Caenorhabditis elegans glutamate-gated chloride channel subunit GluCl responds to glutamate as a homomeric channel while the GluCl subunit is insensitive. A chimera between GluCl and GluCl was used to suggest that major determinants for glutamate binding are present on the GluCl N terminus. Amino acid substitutions in the presumed pore of GluCl conferred direct glutamate gating indicating that GluCl is deficient in coupling of ligand binding to channel gating. Heteromeric channels of GluCl+ may differ from the prototypic muscle nicotinic acetylcholine receptor in that they have the potential to bind ligand to all of the subunits forming the channel.

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