Dynamic interaction of stargazin-like TARPs with cycling AMPA receptors at synapses
Dynamic interaction of stargazin-like TARPs with cycling AMPA receptors at synapses
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DOI：
10.1126/science.1090262
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发表时间：
2004-03-05
期刊：
影响因子：
56.9
通讯作者：
Bredt, DS
中科院分区：
文献类型：
--
作者：
Tomita, S;Fukata, M;Bredt, DS
大脑中活动依赖性可塑性部分源于突触 AMPA 受体数量的变化。 AMPA 受体的突触运输由 stargazin 和同源跨膜 AMPA 受体调节蛋白 (TARP) 控制。我们发现 TARP 在质膜上是稳定的，而 AMPA 受体以谷氨酸调节的方式内化。与 AMPA 受体的相互作用涉及 TARP 的细胞外和细胞内决定因素。与谷氨酸结合后，AMPA 受体与 TARP 分离。这不需要离子流或细胞内第二信使。 AMPA 受体从 TARP 解离的这种变构机制可能参与突触可塑性中谷氨酸介导的受体内化。
Activity-dependent plasticity in the brain arises in part from changes in the number of synaptic AMPA receptors. Synaptic trafficking of AMPA receptors is controlled by stargazin and homologous transmembrane AMPA receptor regulatory proteins (TARPs). We found that TARPs were stable at the plasma membrane, whereas AMPA receptors were internalized in a glutamate-regulated manner. Interaction with AMPA receptors involved both extra- and intracellular determinants of TARPs. Upon binding to glutamate, AMPA receptors detached from TARPs. This did not require ion flux or intracellular second messengers. This allosteric mechanism for AMPA receptor dissociation from TARPs may participate in glutamate-mediated internalization of receptors in synaptic plasticity.