HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Etter, A. Articles by Arena, J. P. Search for Related Content PubMed PubMed Citation Articles by Etter, A. Articles by Arena, J. P. Social Bookmarking                      What's this?

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

---

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.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				D. K. Vassilatis, J. P. Arena, R. H. A. Plasterk, H. A. Wilkinson, J. M. Schaeffer, D. F. Cully, and L. H. T. Van der Ploeg Genetic and Biochemical Evidence for a Novel Avermectin-sensitive Chloride Channel in Caenorhabditis elegans. ISOLATION AND CHARACTERIZATION J. Biol. Chem., December 26, 1997; 272(52): 33167 - 33174. [Abstract] [Full Text] [PDF]