Heteromultimerization and NMDA receptor-clustering activity of chapsyn-110, a member of the PSD-95 family of proteins

被引:488
作者
Kim, E [1 ]
Cho, KO [1 ]
Rothschild, A [1 ]
Sheng, M [1 ]
机构
[1] BAYLOR COLL MED,DEPT CELL BIOL,HOUSTON,TX 77030
关键词
D O I
10.1016/S0896-6273(00)80284-6
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Chapsyn-110, a novel membrane-associated putative guanylate kinase (MAGUK) that binds directly to N-methyl-D-aspartate (NMDA) receptor and Shaker K+ channel subunits, is 70%-80% identical to, and shares an identical domain organization with, PSD-95/SAP90 and SAP97. In rat brain, chapsyn-110 protein shows a somatodendritic expression pattern that overlaps partly with PSD-95 but that contrasts with the axonal distribution of SAP97. Chapsyn-110 associates tightly with the postsynaptic density in brain, and mediates the clustering of both NMDA receptors and K+ channels in heterologous cells. Indeed, chapsyn-110 and PSD-95 can heteromultimerize with each other and are recruited into the same NMDA receptor and K, channel clusters. Thus, chapsyn-110 and PSD-95 may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signalling proteins.
引用
收藏
页码:103 / 113
页数:11
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