Amino-terminal domains of kainate receptors determine the differential dependence on Neto auxiliary subunits for trafficking
Amino-terminal domains of kainate receptors determine the differential dependence on Neto auxiliary subunits for trafficking
复制标题
红藻氨酸受体的氨基末端结构域决定了对 Neto 辅助亚基运输的不同依赖性。
DOI：
10.1073/pnas.1619253114
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发表时间：
2017-01-31
影响因子：
11.1
通讯作者：
Nicoll, Roger A.
中科院分区：
文献类型：
--
作者：
Sheng, Nengyin;Shi, Yun Stone;Nicoll, Roger A.
The kainate receptor (KAR), a subtype of glutamate receptor, mediates excitatory synaptic responses at a subset of glutamatergic synapses. However, the molecular mechanisms underlying the trafficking of its different subunits are poorly understood. Here we use the CA1 hippocampal pyramidal cell, which lacks KAR-mediated synaptic currents, as a null background to determine the minimal requirements for the extrasynaptic and synaptic expression of the GluK2 subunit. We find that the GluK2 receptor itself, in contrast to GluK1, traffics to the neuronal surface and synapse efficiently and the auxiliary subunits Neto1 and Neto2 caused no further enhancement of these two trafficking processes. However, the regulation of GluK2 biophysical properties by Neto proteins is the same as that of GluK1. We further determine that it is the amino-terminal domains (ATDs) of GluK1 and GluK2 that control the strikingly different trafficking properties between these two receptors. Moreover, the ATDs are critical for synaptic expression of heteromeric receptors at mossy fiber-CA3 synapses and also mediate the differential dependence on Neto proteins for surface and synaptic trafficking of GluK1 and GluK2. These results highlight the fundamental differences between the two major KAR subunits and their interplay with Neto auxiliary proteins.
