Importance of Arg‐219 for correct biogenesis of α1 homooligomeric glycine receptors

FEBS Letters

Langosch, Dieter¹  Schmieden, Volker¹  Herbold, Astrid¹  Borman, Joachim¹  Kirsch, Joachim¹ 

[1] Max-Planck-Institut für Hirnforschung, Deutschordenstraβe 46, 60528 Frankfurt, Germany

关键词: Glycine receptor;    Receptor biogenesis;    Transmembrane segment;   

DOI  :  10.1016/0014-5793(93)80872-R

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The inhibitory glycine receptor is characterized by a pentameric arrangement ofsubunits with four predicted transmembrane segments (M1-M4) each. Here, we have mutagenized arginine residues located at both termini of the α1 subunit segment, M2, which lines the receptor's anion channel. No glycine-gated channel formation could be detected in the plasma membrane of expressing cells for any of the mutants. In addition, mutating the arginine at the cytoplasmic terminus of M2 (R219) generated proteins which were only core-glycosylated, retained within intracellular compartments, and aggregated to high molecular weight complexes. Thus, residue R219, which corresponds to an arginine/lysine conserved in other ligand-gated ion channel polypeptides, is essential for correct biogenesis of the receptor.

【 授权许可】

Unknown