The modulation of the postsynaptic signaling machinery by protein phosphorylation has attracted much interest since it is key for the understanding of the regulation of a variety of synaptic functions. While advances in mass spectrometry have allowed us to begin performing large-scale analysis of protein phosphorylation in components of the PSD, the systematic collection of datasets and their functional significance within the context of regulatory signaling networks is in its infancy. Here, we will focus on the composition of the PSD phosphoproteome describing kinase, phosphatase, and protein domain modules involved in the regulation of phosphorylation signaling. We will discuss the impact of synaptic plasticity mechanisms such as long-term potentiation (LTP) in mammalian kinomes and describe the general rules of signaling organization in the PSD phosphoproteome.

中文翻译：

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突触后磷酸化网络的调节机制。

通过蛋白质磷酸化对突触后信号传导机制的调节引起了人们的广泛兴趣，因为它是理解各种突触功能调节的关键。虽然质谱技术的进步使我们能够开始对 PSD 成分中的蛋白质磷酸化进行大规模分析，但数据集的系统收集及其在调控信号网络背景下的功能意义仍处于起步阶段。在这里，我们将重点关注 PSD 磷酸化蛋白质组的组成，描述参与磷酸化信号传导调节的激酶、磷酸酶和蛋白质结构域模块。我们将讨论突触可塑性机制（例如哺乳动物激酶组中的长时程增强 (LTP)）的影响，并描述 PSD 磷酸蛋白质组中信号传导组织的一般规则。