Division of Anatomy, Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Department of Neuroscience, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Brain Struct Funct. 2019 Mar;224(2):521-532. doi: 10.1007/s00429-018-1782-2. Epub 2018 Oct 30.
The SNARE protein SNAP-25 is well documented as regulator of presynaptic vesicle exocytosis. Increasing evidence suggests roles for SNARE proteins in postsynaptic trafficking of glutamate receptors as a basic mechanism in synaptic plasticity. Despite these indications, detailed quantitative subsynaptic localization studies of SNAP-25 have never been performed. Here, we provide novel electron microscopic data of SNAP-25 localization in postsynaptic spines. In addition to its expected presynaptic localization, we show that the protein is also present in the postsynaptic density (PSD), the postsynaptic lateral membrane and on small vesicles in the postsynaptic cytoplasm. We further investigated possible changes in synaptic SNAP-25 protein expression after hippocampal long-term potentiation (LTP). Quantitative analysis of immunogold-labeled electron microscopy sections did not show statistically significant changes of SNAP-25 gold particle densities 1 h after LTP induction, indicating that local trafficking of SNAP-25 does not play a role in the early phases of LTP. However, the strong expression of SNAP-25 in postsynaptic plasma membranes suggests a function of the protein in postsynaptic vesicle exocytosis and a possible role in hippocampal synaptic plasticity.
突触相关膜蛋白 SNAP-25 作为调控神经递质释放的关键蛋白已被广泛研究。越来越多的证据表明,SNARE 蛋白在谷氨酸受体的突触后转运中发挥作用,这是突触可塑性的基本机制。尽管有这些迹象,但对突触后 SNAP-25 的详细亚细胞定位的定量研究尚未进行。在这里,我们提供了突触后棘突中 SNAP-25 定位的新电子显微镜数据。除了预期的突触前定位外,我们还发现该蛋白也存在于突触后密度(PSD)、突触后侧膜和突触后细胞质中的小泡上。我们进一步研究了海马体长时程增强(LTP)后突触 SNAP-25 蛋白表达的可能变化。免疫金标记电子显微镜切片的定量分析显示,LTP 诱导 1 小时后 SNAP-25 金颗粒密度没有统计学上的显著变化,这表明 SNAP-25 的局部转运在 LTP 的早期阶段不起作用。然而,SNAP-25 在突触后质膜中的强表达表明该蛋白在突触后囊泡胞吐作用中的功能,并可能在海马体突触可塑性中发挥作用。