Binding of neuroligins to PSD-95

Binding of neuroligins to PSD-95
复制标题

DOI:
10.1126/science.277.5331.1511
复制
发表时间:
1997-09-05
期刊:
影响因子:
56.9
通讯作者:
Sudhof, TC
Sudhof, TC
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Irie, M;Hata, Y;Sudhof, TC

文献摘要

被引文献

相似文献

PSD-95是中枢突触突触后密度的一种成分,它含有三个PDZ结构域,定位于N-甲基-D-天冬氨酸受体亚单位2(NMDA2受体)和K+通道通向突触。在小鼠前脑中,PSD-95与神经连接蛋白的胞浆COOH末端结合,神经连接蛋白是神经细胞黏附分子,与β-Neurexins相互作用并形成细胞间连接。神经连接素与PSD-95的第三个PDZ结构域结合,而NMDA2受体和K+通道与第一和第二个PDZ结构域相互作用。因此,PSD-95的不同PDZ结构域专门用于不同的功能。PSD-95可以将离子通道和神经递质受体招募到神经连接蛋白和β-神经氨酸形成的神经元之间的细胞间连接。
PSD-95 is a component of postsynaptic densities in central synapses, It contains three PDZ domains that localize N-methyl-D-aspartate receptor subunit 2 (NMDA2 receptor) and K+ channels to synapses. In mouse forebrain, PSD-95 bound to the cytoplasmic COOH-termini of neuroligins, which are neuronal cell adhesion molecules that interact with beta-neurexins and form intercellular junctions. Neuroligins bind to the third PDZ domain of PSD-95, whereas NMDA2 receptors and K+ channels interact with the first and second PDZ domains. Thus different PDZ domains of PSD-95 are specialized for distinct functions. PSD-95 may recruit ion channels and neurotransmitter receptors to intercellular junctions formed between neurons by neuroligins and beta-neurexins.