Baucum Anthony J
Department of Biology, Stark Neurosciences Research Institute, Indiana University-Purdue University Indianapolis , 723 W. Michigan St., Indianapolis, Indiana 46202, United States.
ACS Chem Neurosci. 2017 Apr 19;8(4):689-701. doi: 10.1021/acschemneuro.7b00008. Epub 2017 Feb 23.
Normal neuronal communication and synaptic plasticity at glutamatergic synapses requires dynamic regulation of postsynaptic molecules. Protein expression and protein post-translational modifications regulate protein interactions that underlie this organization. In this Review, we highlight data obtained over the last 20 years that have used qualitative and quantitative proteomics-based approaches to identify postsynaptic protein complexes. Herein, we describe how these proteomics studies have helped lay the foundation for understanding synaptic physiology and perturbations in synaptic signaling observed in different pathologies. We also describe emerging technologies that can be useful in these analyses. We focus on protein complexes associated with the highly abundant and functionally critical proteins: calcium/calmodulin-dependent protein kinase II, the N-methyl-d-aspartate, and α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid glutamate receptors, and postsynaptic density protein of 95 kDa.
谷氨酸能突触处正常的神经元通讯和突触可塑性需要对突触后分子进行动态调节。蛋白质表达和蛋白质翻译后修饰调节构成这种组织基础的蛋白质相互作用。在本综述中，我们重点介绍过去20年中通过基于定性和定量蛋白质组学的方法获得的数据，这些方法用于鉴定突触后蛋白质复合物。在此，我们描述了这些蛋白质组学研究如何为理解突触生理学以及在不同病理中观察到的突触信号扰动奠定基础。我们还描述了可用于这些分析的新兴技术。我们专注于与高度丰富且功能关键的蛋白质相关的蛋白质复合物：钙/钙调蛋白依赖性蛋白激酶II、N-甲基-D-天冬氨酸和α-氨基-3-羟基-5-甲基-4-异恶唑丙酸谷氨酸受体，以及95 kDa的突触后致密蛋白。
