Tomosyn guides SNARE complex formation in coordination with Munc18 and Munc13

被引：14

作者：

Li, Yun ^{[1
]}

Wang, Shen ^{[1
]}

Li, Tianzhi ^{[1
]}

Zhu, Le ^{[1
]}

Ma, Cong ^{[1
,2
]}

机构：

[1] Huazhong Univ Sci & Technol, Minist Educ, Key Lab Mol Biophys, Coll Life Sci & Technol, Luoyu Rd 1037, Wuhan 430074, Hubei, Peoples R China

[2] Huazhong Univ Sci & Technol, Inst Brain Res, Collaborat Innovat Ctr Brain Sci, Wuhan, Hubei, Peoples R China

来源：

FEBS LETTERS | 2018年 / 592卷 / 07期

基金：

中国国家自然科学基金;

关键词：

membrane fusion; Munc13; SNARE complex assembly; synaptic exocytosis; tomosyn; MEMBRANE-FUSION; PROTEIN; SYNTAXIN; EXOCYTOSIS; RELEASE; CORE; ACTIVATION; TEMPLATE; DOMAINS; FORMS;

D O I：

10.1002/1873-3468.13018

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

As a SNARE binding protein, tomosyn has been reported to negatively regulate synaptic exocytosis via arresting syntaxin-1 and SNAP-25 into a nonfusogenic product that precludes synaptobrevin-2 entry, raising the question how the assembly of the SNARE complex is achieved. Here, we have investigated new functions of tomosyn in SNARE complex formation and SNARE-mediated vesicle fusion. Assisted by NSF/alpha-SNAP, syntaxin-1 escapes tomosyn arrest and assembles into the Munc18-1/syntaxin-1 complex. Munc13-1 then catalyzes the transit of syntaxin-1 from the Munc18-1/syntaxin-1 complex to the SNARE complex in a manner specific to synaptobrevin-2 but resistant to tomosyn. Our data suggest that tomosyn ensures SNARE assembly in a way amenable to tight regulation by Munc18-1 and Munc13-1.

引用

页码：1161 / 1172

页数：12

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