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首页> 外文期刊>Neuron >Glutamate-Induced AMPA Receptor Desensitization Increases Their Mobility and Modulates Short-Term Plasticity through Unbinding from Stargazin
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Glutamate-Induced AMPA Receptor Desensitization Increases Their Mobility and Modulates Short-Term Plasticity through Unbinding from Stargazin

机译：谷氨酸诱导的AMPA受体脱敏通过从Stargazin解除结合来增加其移动性并调节短期可塑性

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摘要

Short-term plasticity of AMPAR currents during high-frequency stimulation depends not only on presynaptic transmitter release and postsynaptic AMPAR recovery from desensitization, but also on fast AMPAR diffusion. How AMPAR diffusion within the synapse regulates synaptic transmission on the millisecond scale remains mysterious. Using single-molecule tracking, we found that, upon glutamate binding, synaptic AMPAR diffuse faster. Using AMPAR stabilized in different conformational states by point mutations and pharmacology, we show that desensitized receptors bind less stargazin and are less stabilized at the synapse than receptors in opened or closed-resting states. AMPAR mobility-mediated regulation of short-term plasticity is abrogated when the glutamate-dependent loss in AMPAR-stargazin interaction is prevented. We propose that transition from the activated to the desensitized state leads to partial loss in AMPAR-stargazin interaction that increases AMPAR mobility and allows faster recovery from desensitization-mediated synaptic depression, without affecting the overall nano-organization of AMPAR in synapses.
机译：高频刺激期间AMPAR电流的短期可塑性不仅取决于突触前递质的释放和脱敏后突触后AMPAR的恢复，还取决于AMPAR的快速扩散。突触中AMPAR的扩散如何在毫秒级调节突触传递仍然是个谜。使用单分子跟踪，我们发现，在谷氨酸结合后，突触AMPAR扩散得更快。使用通过点突变和药理作用稳定在不同构象状态的AMPAR，我们发现脱敏受体与处于开放状态或闭合休息状态的受体相比，结合较少的stargazin，并且在突触中的稳定性较低。当防止谷氨酸依赖于AMPAR-stargazin相互作用的丧失时，可废除AMPAR流动性介导的短期可塑性调节。我们建议从激活状态到脱敏状态的过渡导致AMPAR-stargazin相互作用的部分丧失，这会增加AMPAR的活动性并允许从脱敏介导的突触抑制中更快恢复，而不会影响突触中AMPAR的整体纳米组织。

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