Division of Experimental & Translational Neuroscience, Krembil Brain Institute, University Health Network, Toronto, ON, Canada.
Faculty of Medicine, Department of Physiology, University of Toronto, Toronto, ON, Canada.
Adv Neurobiol. 2023;33:233-254. doi: 10.1007/978-3-031-34229-5_9.
Soluble NSF attachment protein receptor (SNARE) proteins play a central role in synaptic vesicle (SV) exocytosis. These proteins include the vesicle-associated SNARE protein (v-SNARE) synaptobrevin and the target membrane-associated SNARE proteins (t-SNAREs) syntaxin and SNAP-25. Together, these proteins drive membrane fusion between synaptic vesicles (SV) and the presynaptic plasma membrane to generate SV exocytosis. In the presynaptic active zone, various proteins may either enhance or inhibit SV exocytosis by acting on the SNAREs. Among the inhibitory proteins, tomosyn, a syntaxin-binding protein, is of particular importance because it plays a critical and evolutionarily conserved role in controlling synaptic transmission. In this chapter, we describe how tomosyn was discovered, how it interacts with SNAREs and other presynaptic regulatory proteins to regulate SV exocytosis and synaptic plasticity, and how its various domains contribute to its synaptic functions.
可溶性 NSF 附着蛋白受体 (SNARE) 蛋白在突触小泡 (SV) 胞吐作用中发挥核心作用。这些蛋白质包括囊泡相关 SNARE 蛋白 (v-SNARE) 突触融合蛋白和靶膜相关 SNARE 蛋白 (t-SNAREs) 突触融合蛋白和 SNAP-25。这些蛋白质共同驱动突触小泡 (SV) 和突触前质膜之间的膜融合，从而产生 SV 胞吐作用。在突触前活性区，各种蛋白质可以通过作用于 SNARE 来增强或抑制 SV 胞吐作用。在抑制性蛋白质中，突触融合蛋白结合蛋白 tomosyn 尤为重要，因为它在控制突触传递中发挥着关键的、进化上保守的作用。在本章中，我们将描述 tomosyn 是如何被发现的，它如何与 SNARE 及其他突触前调节蛋白相互作用来调节 SV 胞吐作用和突触可塑性，以及它的不同结构域如何贡献其突触功能。
