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

Heteromultimerization and NMDA receptor-clustering activity of chapsyn-110, a member of the PSD-95 family of proteins
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DOI:
10.1016/s0896-6273(00)80284-6
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发表时间:
1996-07-01
期刊:
影响因子:
16.2
通讯作者:
Sheng, M
Sheng, M
中科院分区:
医学1区
文献类型:
--
作者:
Kim, E;Cho, KO;Sheng, M

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Chaopn-110是一种与N-甲基-D-天冬氨酸(NMDA)受体和Shaker K+通道亚基直接结合的新型膜相关鸟氨酸激酶(MAGUK),与PSD-95/SAP90和SAP97有70%-80%的同源性和相同的结构域组织。在大鼠脑中,Chaopn-110蛋白显示出与PSD-95部分重叠但与SAP97轴突分布相反的体树突状表达模式。CHAPECN-110与脑内突触后密度密切相关,并介导NMDA受体和K+通道在异种细胞中的聚集。实际上,chaopn-110和PSD-95可以相互异构化,并被招募到相同的NMDA受体和K通道簇中。因此,Chaopn-110和PSD-95可能在突触后位置相互作用,形成一个多聚体支架,用于聚集受体、离子通道和相关的信号蛋白。
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.