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突触可塑性中AMPAR-TARP复合物的磷酸化作用

Phosphorylation of the AMPAR-TARP Complex in Synaptic Plasticity.

作者信息

Park Joongkyu

机构信息

Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA.

Department of Neurology, Wayne State University School of Medicine, Detroit, MI 48201, USA.

出版信息

Proteomes. 2018 Oct 8;6(4):40. doi: 10.3390/proteomes6040040.

DOI:10.3390/proteomes6040040
PMID:30297624
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6313930/
Abstract

Synaptic plasticity has been considered a key mechanism underlying many brain functions including learning, memory, and drug addiction. An increase or decrease in synaptic activity of the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) complex mediates the phenomena as shown in the cellular models of synaptic plasticity, long-term potentiation (LTP), and depression (LTD). In particular, protein phosphorylation shares the spotlight in expressing the synaptic plasticity. This review summarizes the studies on phosphorylation of the AMPAR pore-forming subunits and auxiliary proteins including transmembrane AMPA receptor regulatory proteins (TARPs) and discusses its role in synaptic plasticity.

摘要

突触可塑性被认为是许多脑功能（包括学习、记忆和药物成瘾）的关键机制。α-氨基-3-羟基-5-甲基-4-异恶唑丙酸受体（AMPAR）复合物突触活性的增加或减少介导了突触可塑性、长时程增强（LTP）和长时程抑制（LTD）细胞模型中所示的现象。特别是，蛋白质磷酸化在表达突触可塑性方面备受关注。本综述总结了关于AMPAR孔形成亚基和辅助蛋白（包括跨膜AMPA受体调节蛋白（TARPs））磷酸化的研究，并讨论了其在突触可塑性中的作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ca47/6313930/25acf15d8858/proteomes-06-00040-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ca47/6313930/4e585afd1092/proteomes-06-00040-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ca47/6313930/25acf15d8858/proteomes-06-00040-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ca47/6313930/4e585afd1092/proteomes-06-00040-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ca47/6313930/25acf15d8858/proteomes-06-00040-g002.jpg

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本文引用的文献

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