动力蛋白-1 与天然小鼠脑 BKCa 通道共结合：突触蛋白复合物的蛋白质组学分析。
Dynamin-1 co-associates with native mouse brain BKCa channels: proteomics analysis of synaptic protein complexes.
机构信息
Waggoner Center for Alcohol and Addiction Research, College of Natural Sciences, The University of Texas at Austin, Austin, TX 78712, USA.
出版信息
FEBS Lett. 2010 Mar 5;584(5):845-51. doi: 10.1016/j.febslet.2009.12.061. Epub 2010 Jan 29.
Abstract
In every synapse, a large number of proteins interact with other proteins in order to carry out signaling and transmission in the central nervous system. In this study, we used interaction proteomics to identify novel synaptic protein interactions in mouse cortical membranes under native conditions. Using immunoprecipitation, immunoblotting, and mass spectrometry, we identified a number of novel synaptic protein interactions involving soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), calcium-activated potassium channel (BKCa) alpha subunits, and dynamin-1. These novel interactions offer valuable insight into the protein-protein interaction network in intact synapses that could advance understanding of vesicle trafficking, release, and recycling.
摘要
在每个突触中，大量的蛋白质与其他蛋白质相互作用，以在中枢神经系统中进行信号传递和传输。在这项研究中，我们使用相互作用蛋白质组学来鉴定在天然条件下，小鼠皮质膜中的新型突触蛋白相互作用。通过免疫沉淀、免疫印迹和质谱分析，我们鉴定出了一些涉及可溶性 N-乙基马来酰亚胺敏感因子附着蛋白受体 (SNAREs)、钙激活钾通道 (BKCa) α亚基和动力蛋白-1 的新型突触蛋白相互作用。这些新的相互作用为完整突触中的蛋白质-蛋白质相互作用网络提供了有价值的见解，这可能有助于理解囊泡运输、释放和再循环。
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