Distinct Subunit Domains Govern Synaptic Stability and Specificity of the Kainate Receptor.
Distinct Subunit Domains Govern Synaptic Stability and Specificity of the Kainate Receptor.
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DOI：
10.1016/j.celrep.2016.05.093
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发表时间：
2016-07-12
期刊：
影响因子：
8.8
通讯作者：
Tomita S
中科院分区：
文献类型：
--
作者：
Straub C;Noam Y;Nomura T;Yamasaki M;Yan D;Fernandes HB;Zhang P;Howe JR;Watanabe M;Contractor A;Tomita S
神经元之间的突触通信需要神经递质受体精确定位到正确的突触类型。红藻氨酸盐型谷氨酸受体具有受限的突触定位，其由传入突触前连接决定。控制这种输入特异性突触定位的机制仍不清楚。在这里，我们研究如何亚基组成和特定的亚基结构域有助于红藻氨酸受体的突触定位。GluK 2低亲和力亚基的胞质结构域稳定了突触处的红藻氨酸受体。相比之下，GluK 4/5高亲和力亚基的细胞外结构域通过与C1 q样蛋白的相互作用协同控制红藻氨酸受体的突触特异性。因此，天然红藻氨酸受体复合物的输入特异性突触定位涉及两种机制，这两种机制是突触处受体的特异性和稳定性的基础。
Synaptic communication between neurons requires the precise localization of neurotransmitter receptors to the correct synapse type. Kainate-type glutamate receptors have restricted synaptic localization that is determined by the afferent presynaptic connection. The mechanisms that govern this input-specific synaptic localization remain unclear. Here we examine how subunit composition and specific subunit domains contribute to synaptic localization of kainate receptors. The cytoplasmic domain of the GluK2 low-affinity subunit stabilized kainate receptors at synapses. In contrast, the extracellular domain of the GluK4/5 high-affinity subunit synergistically controls the synaptic specificity of kainate receptors through interaction with C1q-like proteins. Thus the input-specific synaptic localization of the native kainate receptor complex involves two mechanisms that underlie specificity and stabilization of the receptor at synapses.