SNARE (Soluble NSF(N-ethylmaleimide-sensitive factor) Attachment Receptor) complex is a trimeric supramolecular organization of SNAP25, syntaxin, and VAMP which mediates fusion of synaptic vesicles with the presynaptic plasma membrane. The functioning of this entire protein assembly is dependent on its tetrahelical coiled coil structure alongside its interaction with a large spectrum of regulatory proteins like synaptotagmin, complexin, intersectin, etc. Defects arising in SNARE complex assembly due to mutations or faulty post-translational modifications are associated to severe synaptopathies like Schizophrenia and also proteopathies like Alzheimer's disease. The review primarily focuses on SNAP25, which is the prime contributor in the complex assembly. It is conceptualized that the network of protein interactions of this helical protein assists as a chaperoning system for attaining functional structure. Additionally, the innate disordered nature of SNAP25 and its amyloidogenic propensities have been highlighted employing computational methods. The intrinsic nature of SNAP25 is anticipated to form higher-order aggregates due to its cysteine rich domain, which is also a target for several post-translational modifications. Furthermore, the aberrations in the structure and expression profile of the protein display common patterns in the pathogenesis of a diverse synaptopathies and proteopathies. This work of SNARE literature aims to provide a new comprehensive outlook and research directions towards SNARE complex and presents SNAP25 as a common neuropathological hallmark which can be a diagnostic or therapeutic target.

中文翻译：

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神经元SNARE复合体：具有复杂的蛋白质与蛋白质相互作用的蛋白质折叠系统，其共同的神经病理学特征为SNAP25。

SNARE（可溶性NSF（N-乙基马来酰亚胺敏感因子）附着受体）复合物是SNAP25，syntaxin和VAMP的三聚体超分子组织，介导突触小泡与突触前质膜的融合。整个蛋白质装配体的功能取决于其四螺旋盘绕的螺旋结构，以及与大量调节蛋白如突触结合蛋白，复合蛋白，intersectin等的相互作用。由于突变或错误的翻译后修饰，SNARE复杂装配体中产生的缺陷是与严重的突触病（如精神分裂症）和蛋白病（如阿尔茨海默氏病）有关。审查主要集中在SNAP25，SNAP25是复杂装配中的主要贡献者。从概念上讲，这种螺旋蛋白质的蛋白质相互作用网络有助于获得功能结构的伴侣系统。此外，SNAP25的先天无序性及其淀粉样蛋白生成倾向已采用计算方法进行了强调。由于其富含半胱氨酸的结构域，SNAP25的内在性质有望形成更高阶的聚集体，这也是几种翻译后修饰的目标。此外，蛋白质的结构和表达谱中的畸变在多种突触病和蛋白病的发病机理中显示出共同的模式。