Subtype-specific assembly of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their N-terminal domains

被引:92
作者
Leuschner, WD [1 ]
Hoch, W [1 ]
机构
[1] Max Planck Inst Entwicklungsbiol, Biochem Abt, D-72076 Tubingen, Germany
关键词
D O I
10.1074/jbc.274.24.16907
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Glutamate receptors (GluR) are oligomeric protein complexes formed by the assembly of four or perhaps five subunits, The rules that govern the selectivity of this process are not well understood. Here, we expressed combinations of subunits from two related GluR subfamilies in COS7 cells, the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and kainate receptors. By co-immunoprecipitation experiments, we assessed the ability of AMPA receptor subunits to assemble into multimeric complexes. Subunits GluR1-4 associated with indistinguishable efficiency with each other, whereas the kainate receptor subunits GluR6 and 7 showed a much lower degree of association with GluR1, Using chimeric receptors and truncation fragments of subunits, we show that this assembly specificity is determined by N-terminal regions of these subunits and that the most N-terminal domain of GluR2 together with a membrane anchor efficiently associates with GLuR1.
引用
收藏
页码:16907 / 16916
页数:10
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