Proteasome regulates the mediators of cytoplasmic polyadenylation signaling during late-phase long-term potentiation.
Proteasome regulates the mediators of cytoplasmic polyadenylation signaling during late-phase long-term potentiation.
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DOI：
10.1016/j.neulet.2014.09.038
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发表时间：
2014-11-07
影响因子：
2.5
通讯作者：
Hegde AN
中科院分区：
文献类型：
--
作者：
Dong C;Vashisht A;Hegde AN
泛素-蛋白酶体通路对于突触的长期可塑性是必不可少的，但其确切的作用尚不清楚。以前，我们建立了蛋白酶体抑制增加了早期，诱导部分的晚期相长时程增强（L-LTP），但块的后期，维持部分。我们先前的工作也表明，蛋白酶体调节哺乳动物靶向雷帕霉素途径的组分进行翻译。在这项研究中，我们测试了蛋白酶体在调节L-LTP翻译所需的细胞质多聚腺苷酸化信号转导中的可能作用。我们发现，多聚腺苷酸化抑制剂虫草素减少了蛋白酶体抑制介导的早期L-LTP的增强。此外，阻断Aurora-A激酶和钙-钙调蛋白依赖性激酶II可减少蛋白酶体抑制引起的早期L-LTP增加。我们的研究结果表明，在诱导长期突触可塑性的过程中，多聚腺苷酸化介导的翻译控制和蛋白质降解之间存在联系。
The ubiquitin-proteasome pathway is essential for long-term synaptic plasticity, but its exact roles remain unclear. Previously we established that proteasome inhibition increased the early, induction part of late-phase long-term potentiation (L-LTP) but blocks the late, maintenance part. Our prior work also showed that the proteasome modulates components of the mammalian target of rapamycin pathway for translation. In this study, we tested the possible role of the proteasome in regulating the cytoplasmic polyadenylation signaling required for translation during L-LTP. We found that a polyadenylation inhibitor cordycepin diminishes the enhancement of early L-LTP mediated by proteasome inhibition. Furthermore, blocking Aurora-A kinase and calcium-calmodulin-dependent kinase II reduces the increase in early L-LTP brought about by proteasome inhibition. Our results suggest a link between polyadenylation-mediated translational control and protein degradation during induction of long-term synaptic plasticity.
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