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Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry.

Kuhse, J. and Laube, Bodo and Magalei, D. and Betz, H. (1993):
Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry.
In: Neuron, (6), 11. pp. 1049-56, ISSN 0896-6273,
[Article]

Abstract

The inhibitory glycine receptor (GlyR) is a pentameric protein composed of two types (alpha and beta) of membrane-spanning subunits. Coexpression in Xenopus oocytes of a low affinity mutant of the alpha 2 subunit with the alpha 1 and beta subunits indicated that GlyRs assembled from alpha 1 and alpha 2 polypeptides contain variable subunit ratios, whereas alpha/beta hetero-oligomers have an invariant (3:2) stoichiometry. Analysis of different alpha/beta chimeric constructs revealed that this difference in assembly behavior is mediated by the N-terminal extracellular regions of the receptor subunits. Substitution of residues diverging between the alpha and beta subunits identified combinations of sequence motifs determining subunit stoichiometry.

Item Type: Article
Erschienen: 1993
Creators: Kuhse, J. and Laube, Bodo and Magalei, D. and Betz, H.
Title: Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry.
Language: English
Abstract:

The inhibitory glycine receptor (GlyR) is a pentameric protein composed of two types (alpha and beta) of membrane-spanning subunits. Coexpression in Xenopus oocytes of a low affinity mutant of the alpha 2 subunit with the alpha 1 and beta subunits indicated that GlyRs assembled from alpha 1 and alpha 2 polypeptides contain variable subunit ratios, whereas alpha/beta hetero-oligomers have an invariant (3:2) stoichiometry. Analysis of different alpha/beta chimeric constructs revealed that this difference in assembly behavior is mediated by the N-terminal extracellular regions of the receptor subunits. Substitution of residues diverging between the alpha and beta subunits identified combinations of sequence motifs determining subunit stoichiometry.

Journal or Publication Title: Neuron
Journal volume: 11
Number: 6
Divisions: 10 Department of Biology
10 Department of Biology > Neurophysiology and Neurosensory Systems
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Date Deposited: 12 Apr 2011 11:27
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