Dosemeci Ayse, Toy Dana, Burch Amelia, Bayer K Ulrich, Tao-Cheng Jung-Hwa
Laboratory of Neurobiology, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, USA.
Department of Pharmacology, School of Medicine, University of Colorado Denver, Aurora, CO, USA.
FEBS Lett. 2016 Sep;590(17):2934-9. doi: 10.1002/1873-3468.12334. Epub 2016 Aug 20.
Ankyrin repeat and sterile alpha motif domain-containing protein 1B (ANKS1B, also known as AIDA-1) is a major component of the postsynaptic density (PSD) in excitatory neurons where it concentrates at the electron-dense core under basal conditions and moves out during activity. This study investigates the molecular mechanism underlying activity-induced displacement of AIDA-1. Experiments with PSD fractions from brain indicate phosphorylation of AIDA-1 upon activation of endogenous CaMKII. Immuno-electron microscopy studies show that treatment of hippocampal neurons with NMDA results in an ~ 30 nm shift in the median distance of the AIDA-1 label from the postsynaptic membrane, an effect that is blocked by the CaMKII inhibitor tatCN21. CaMKII-mediated redistribution of AIDA-1 is similar to that observed for SynGAP. CaMKII-mediated removal of two abundant PSD-95-binding proteins from the PSD core during activity is expected to initiate a molecular reorganization at the PSD.
锚蛋白重复序列和无活性α基序结构域蛋白1B（ANKS1B，也称为AIDA-1）是兴奋性神经元突触后致密物（PSD）的主要成分，在基础条件下它集中于电子致密核心，而在活动期间移出。本研究调查了AIDA-1活性诱导移位的分子机制。来自脑的PSD组分的实验表明，内源性CaMKII激活后AIDA-1发生磷酸化。免疫电子显微镜研究显示，用NMDA处理海马神经元会导致AIDA-1标记与突触后膜的中位距离发生约30nm的移位，该效应被CaMKII抑制剂tatCN21阻断。CaMKII介导的AIDA-1重新分布与SynGAP的相似。活动期间CaMKII介导从PSD核心去除两种丰富的PSD-95结合蛋白，预计会引发PSD处的分子重组。
