ASSEMBLY OF THE INHIBITORY GLYCINE RECEPTOR - IDENTIFICATION OF AMINO-ACID-SEQUENCE MOTIFS GOVERNING SUBUNIT STOICHIOMETRY

被引：152

作者：

KUHSE, J

LAUBE, B

MAGALEI, D

BETZ, H

机构：

[1] Department of Neurochemistry Max-Planck-Institute for Brain Research, 60528 Frankfurt

来源：

NEURON | 1993年 / 11卷 / 06期

关键词：

D O I：

10.1016/0896-6273(93)90218-G

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

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 alpha2 subunit with the alpha1 and beta subunits indicated that GlyRs assembled from alpha1 and alpha2 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.

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页码：1049 / 1056

页数：8

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