Molecular constituents and phosphorylation-dependent regulation of the post-synaptic density

被引：58

作者：

Yamauchi, T ^{[1
]}

机构：

[1] Univ Tokushima, Fac Pharmaceut Sci, Dept Biochem, Tokushima 7708505, Japan

来源：

MASS SPECTROMETRY REVIEWS | 2002年 / 21卷 / 04期

关键词：

Ca2+/calmodulin-dependent protein kinase II; (CaM KII); post-synaptic density; phosphorylation; synaptic plasticity; long-term potentiation; glutamate receptor; proteomics analysis;

D O I：

10.1002/mas.10033

中图分类号：

O433 [光谱学];

学科分类号：

0703 ; 070302 ;

摘要：

The post-synaptic density (PSD) contains receptors with associated signaling- and scaffolding-proteins that organize signal-transduction pathways near the post-synaptic membrane. The PSD plays an important role in synaptic plasticity, and protein phosphorylation is critical to the regulation of PSD function, including learning and memory. Recently, studies have investigated the protein constituents of the PSD and substrate proteins for various protein kinases by proteomic analysis. The present review focuses on the molecular properties of PSD proteins, and substrates of protein kinases and their regulation by phosphorylation in order to understand the role of PSD in synaptic plasticity. (C) 2003 Wiley Periodicals, Inc.

引用

页码：266 / 286

页数：21

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