Synaptobrevin2 monomers and dimers differentially engage to regulate the functional trans-SNARE assembly.

IF 3.3 2区 生物学 Q1 BIOLOGY
Life Science Alliance Pub Date : 2024-01-18 Print Date: 2024-04-01 DOI:10.26508/lsa.202402568
Swapnali S Patil, Kinjal Sanghrajka, Malavika Sriram, Aritra Chakraborty, Sougata Majumdar, Bhavya R Bhaskar, Debasis Das
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引用次数: 0

Abstract

The precise cell-to-cell communication relies on SNARE-catalyzed membrane fusion. Among ∼70 copies of synaptobrevin2 (syb2) in synaptic vesicles, only ∼3 copies are sufficient to facilitate the fusion process at the presynaptic terminal. It is unclear what dictates the number of SNARE complexes that constitute the fusion pore assembly. The structure-function relation of these dynamic pores is also unknown. Here, we demonstrate that syb2 monomers and dimers differentially engage in regulating the trans-SNARE assembly during membrane fusion. The differential recruitment of two syb2 structures at the membrane fusion site has consequences in regulating individual nascent fusion pore properties. We have identified a few syb2 transmembrane domain residues that control monomer/dimer conversion. Overall, our study indicates that syb2 monomers and dimers are differentially recruited at the release sites for regulating membrane fusion events.

Synaptobrevin2单体和二聚体以不同方式参与调节功能性跨SNARE组装。
细胞间的精确交流依赖于 SNARE 催化的膜融合。在突触小泡中的 70 个突触素 2(syb2)拷贝中,只有 3 个拷贝足以促进突触前末端的融合过程。目前还不清楚是什么决定了构成融合孔装配的 SNARE 复合物的数量。这些动态孔的结构-功能关系也不清楚。在这里,我们证明了 syb2 单体和二聚体在膜融合过程中以不同方式参与调节反式 SNARE 组装。两种 syb2 结构在膜融合位点的不同招募会对新生融合孔的个体特性产生影响。我们发现了一些控制单体/二聚体转换的 syb2 跨膜结构域残基。总之,我们的研究表明,syb2单体和二聚体在释放位点的招募方式不同,从而调节膜融合事件。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Life Science Alliance
Life Science Alliance Agricultural and Biological Sciences-Plant Science
CiteScore
5.80
自引率
2.30%
发文量
241
审稿时长
10 weeks
期刊介绍: Life Science Alliance is a global, open-access, editorially independent, and peer-reviewed journal launched by an alliance of EMBO Press, Rockefeller University Press, and Cold Spring Harbor Laboratory Press. Life Science Alliance is committed to rapid, fair, and transparent publication of valuable research from across all areas in the life sciences.
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