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首页> 外文期刊>The European Journal of Neuroscience >Activity-driven mobilization of post-synaptic proteins.
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Activity-driven mobilization of post-synaptic proteins.

机译：突触后蛋白的活动驱动动员。

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摘要

Synapses established during central nervous system development can be modified through synapse elimination and formation. These processes are, in part, activity dependent and require regulated trafficking of post-synaptic components. Here, we investigate the activity-driven remodeling of cultured rat hippocampal neurons at 14 days in vitro, focusing on the post-synaptic proteins PSD-95, Shank, neuroligin (NL)1 and actin. Using live imaging and photoconductive stimulation, we found that high-frequency activity altered the trajectory, but not velocity, of PSD-95-GFP and Shank-YFP clusters, whereas it reduced the speed and increased the number of NL1 clusters. Actin-CFP reorganized into puncta following activity and approximately 50% of new puncta colocalized with NL1 clusters. Actin reorganization was enhanced by the overexpression of NL1 and decreased by the expression of an NL1 mutant, NL1-R473C. These results demonstrate activity-dependent changes that may result in the formation of new post-synaptic sites and suggest that NL1 modulates actin reorganization. The results also suggest that a common mechanism underlies both the developmental and activity-dependent remodeling of excitatory synapses.
机译：在中枢神经系统发育过程中建立的突触可通过消除和形成突触进行修饰。这些过程部分地取决于活动，并且需要经调节的突触后成分的运输。在这里，我们调查培养的大鼠海马神经元在体外14天的活动驱动的重塑，重点是突触后蛋白PSD-95，Shank，neuroligin（NL）1和肌动蛋白。使用实时成像和光导刺激，我们发现高频活动改变了PSD-95-GFP和Shank-YFP簇的轨迹，但没有改变速度，而降低了速度并增加了NL1簇的数量。肌动蛋白-CFP在活动后重新组织成点状，约有50％的新点状与NL1簇共定位。肌动蛋白的重组通过NL1的过表达增强，而通过NL1突变体NL1-R473C的表达降低。这些结果表明活动依赖的变化，可能导致新的突触后网站的形成，并表明NL1调节肌动蛋白的重组。结果还表明，共同机制是兴奋性突触的发育和活动依赖性重塑的基础。

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